PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	Clomiphene	165-175	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
31778586-10	2020	GMDR analyses suggested that a 3-locus model: SLC15A1 rs2297322-PXR rs3732359-FMO3 rs2266782 was an appropriate predictive model of docetaxel-induced myelosuppression (P = .017, Testing Bal.Acc = 0.653, CV Consistency = 10/10).	docetaxel	132-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	78-82
31778586-11	2020	WHAT IS NEW AND CONCLUSION: Our findings suggest multiple novel predictive biomarkers of docetaxel-induced myelosuppression: SLC15A1 rs2297322, PXR rs3732359 and FMO3 rs2266782.	docetaxel	89-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
32653296-0	2020	Novel variants in outer protein surface of flavin-containing monooxygenase 3 found in an Argentinian case with impaired capacity for trimethylamine N-oxygenation.	trimethylamine n	133-149	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-76
32653296-4	2020	Recombinant FMO3 proteins of the wild-type and the novel two variants underwent kinetic analyses of their trimethylamine N-oxygenation activities.	trimethylamine n	106-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-16
32653296-5	2020	P73L; E158K; E308G and F140S FMO3 proteins exhibited moderately and severely decreased trimethylamine N-oxygenation capacities (~50% and ~10% of wild-type FMO3, respectively).	trimethylamine n	87-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-33
32653296-5	2020	P73L; E158K; E308G and F140S FMO3 proteins exhibited moderately and severely decreased trimethylamine N-oxygenation capacities (~50% and ~10% of wild-type FMO3, respectively).	trimethylamine n	87-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	155-159
32653296-8	2020	This is the first report and characterization of a patient of fish odor syndrome caused by genetic aberrations leading to impaired FMO3-dependent N-oxygenation of trimethylamine found in the Argentinian population.	trimethylamine	163-177	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
32587943-2	2020	The trimethylamine N-oxide (TMAO) metaorganismal pathway is the most deeply investigated one, which comprises trimethylamine precursors, such as choline, trimethylamine lyase, trimethylamine, host liver FMO3, TMAO, and downstream effectors involving unfolded protein response (UPR), NF-kappaB and NLRP3 inflammasome.	trimethyloxamine	4-26	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-207
32587943-2	2020	The trimethylamine N-oxide (TMAO) metaorganismal pathway is the most deeply investigated one, which comprises trimethylamine precursors, such as choline, trimethylamine lyase, trimethylamine, host liver FMO3, TMAO, and downstream effectors involving unfolded protein response (UPR), NF-kappaB and NLRP3 inflammasome.	trimethyloxamine	28-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-207
32587943-2	2020	The trimethylamine N-oxide (TMAO) metaorganismal pathway is the most deeply investigated one, which comprises trimethylamine precursors, such as choline, trimethylamine lyase, trimethylamine, host liver FMO3, TMAO, and downstream effectors involving unfolded protein response (UPR), NF-kappaB and NLRP3 inflammasome.	trimethylamine	4-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-207
32587943-2	2020	The trimethylamine N-oxide (TMAO) metaorganismal pathway is the most deeply investigated one, which comprises trimethylamine precursors, such as choline, trimethylamine lyase, trimethylamine, host liver FMO3, TMAO, and downstream effectors involving unfolded protein response (UPR), NF-kappaB and NLRP3 inflammasome.	trimethylamine	110-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-207
32587943-2	2020	The trimethylamine N-oxide (TMAO) metaorganismal pathway is the most deeply investigated one, which comprises trimethylamine precursors, such as choline, trimethylamine lyase, trimethylamine, host liver FMO3, TMAO, and downstream effectors involving unfolded protein response (UPR), NF-kappaB and NLRP3 inflammasome.	trimethyloxamine	209-213	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-207
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	Clomiphene	165-175	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-130
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	Dasatinib	177-186	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	Dasatinib	177-186	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-130
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	GSK5182	188-195	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	GSK5182	188-195	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-130
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	VX680	200-210	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	VX680	200-210	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-130
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	n-oxide	234-241	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
32197603-3	2020	Here, Escherichia coli (E. coli) JM109 cells over-expressing the recombinant human FMO3 (flavin-containing monooxygenase isoform 3) were used for the conversions of clomiphene, dasatinib, GSK5182 and tozasertib to their corresponding N-oxide metabolites.	n-oxide	234-241	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-130
32197603-6	2020	In addition, FMO3 shows high regio-selectivity in metabolizing GSK5182 where only the (Z) isomer is monooxygenated.	GSK5182	63-70	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	13-17
32197603-7	2020	CONCLUSIONS: The study shows the successful use of human FMO3-based whole-cell as a biocatalyst for the efficient synthesis of drug metabolites including regio-selective reactions involving GSK5182, a new candidate against type 2 diabetes mellitus.	GSK5182	190-197	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
31580948-0	2019	Uncoupled human flavin-containing monooxygenase 3 releases superoxide radical in addition to hydrogen peroxide.	Superoxides	59-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-49
31317802-2	2020	The majority of FMO-mediated metabolism in adult human liver is catalyzed by FMO3.	fmo	16-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-81
31317802-7	2020	Elevated plasma concentrations of trimethylamine N-oxide, a product of an FMO3-catalyzed reaction, have been implicated in certain diseases, particularly cardiovascular disease.	trimethyloxamine	34-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	74-78
31543404-4	2019	Furthermore, interventions to reduce TMAO, either by manipulation of the gut microbiota or by inhibition of the TMAO synthesizing enzyme, flavin-containing monooxygenase 3, can reduce PERK activation and FoxO1 levels in the liver.	trimethyloxamine	37-41	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-171
31543404-4	2019	Furthermore, interventions to reduce TMAO, either by manipulation of the gut microbiota or by inhibition of the TMAO synthesizing enzyme, flavin-containing monooxygenase 3, can reduce PERK activation and FoxO1 levels in the liver.	trimethyloxamine	112-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-171
31993760-1	2020	PURPOSE: This prospective study aimed to evaluate the effects of genetic polymorphisms in sulindac-related metabolizing enzyme genes including FMO3 and AOX1 on the population pharmacokinetics of sulindac in 58 pregnant women with preterm labor.	Sulindac	195-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	143-147
31993760-7	2020	In stepwise modeling, gestational age impacted volume of distribution (Vc), and FMO3 rs2266782 was shown by the Michaelis constant to affect conversion of sulindac sulfide to sulindac (KM32); these were retained in the final model.	sulindac sulfide	155-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
31993760-7	2020	In stepwise modeling, gestational age impacted volume of distribution (Vc), and FMO3 rs2266782 was shown by the Michaelis constant to affect conversion of sulindac sulfide to sulindac (KM32); these were retained in the final model.	Sulindac	155-163	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
31993760-8	2020	CONCLUSIONS: Genetic polymorphisms of FMO3 and AOX1 could affect the pharmacokinetics of sulindac in women who undergo preterm labor.	Sulindac	89-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	38-42
31580948-0	2019	Uncoupled human flavin-containing monooxygenase 3 releases superoxide radical in addition to hydrogen peroxide.	Hydrogen Peroxide	93-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-49
31580948-1	2019	Human flavin-containing monooxygenase 3 (hFMO3) is a drug-metabolizing enzyme capable of performing N- or S-oxidation using the C4a-hydroperoxy intermediate.	Nitrogen	100-101	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
31580948-1	2019	Human flavin-containing monooxygenase 3 (hFMO3) is a drug-metabolizing enzyme capable of performing N- or S-oxidation using the C4a-hydroperoxy intermediate.	Nitrogen	100-101	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
31580948-1	2019	Human flavin-containing monooxygenase 3 (hFMO3) is a drug-metabolizing enzyme capable of performing N- or S-oxidation using the C4a-hydroperoxy intermediate.	15-hydroperoxyprostaglandin E2	128-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
31580948-1	2019	Human flavin-containing monooxygenase 3 (hFMO3) is a drug-metabolizing enzyme capable of performing N- or S-oxidation using the C4a-hydroperoxy intermediate.	15-hydroperoxyprostaglandin E2	128-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
31580948-5	2019	For the first time, we were able to follow the production of the superoxide radical in hFMO3, which was found to account for 13-18% of the total uncoupling of this human enzyme.	Superoxides	65-75	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-92
31401033-4	2019	Proband 1 harbored a novel CC deletion resulting in p.[(Pro153Gln fs; Phe166Ter)] FMO3, which was in trans configuration with p.(Cys197Ter).	phe166ter	70-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	82-86
31239195-0	2019	Impact of flavin-containing monooxygenase 3 and CYP2C19 genotypes on plasma disposition and adverse effects of voriconazole administered orally in immunocompromised patients.	Voriconazole	111-123	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	10-43
31239195-1	2019	Flavin-containing monooxygenase (FMO) 3 together with cytochrome P450 (CYP) 2C19 play a significant role in voriconazole N-oxidation.	Voriconazole	108-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-39
31239195-1	2019	Flavin-containing monooxygenase (FMO) 3 together with cytochrome P450 (CYP) 2C19 play a significant role in voriconazole N-oxidation.	Nitrogen	121-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-39
31239195-2	2019	This study aimed to evaluate the influence of FMO3 and CYP2C19 genotypes on the plasma disposition and adverse effects of voriconazole in immunocompromised patients.	Voriconazole	122-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
31239195-6	2019	The patients with FMO3 E158K/E308G had a lower plasma concentration of voriconazole.	Voriconazole	71-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-22
31239195-7	2019	The metabolic ratio to N-oxide was significantly higher in the FMO3 E158K/E308G group than in the wild group.	n-oxide	23-30	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
31239195-13	2019	In conclusion, FMO3 E158K/E308G decreased the plasma concentration of voriconazole through its higher metabolic activity.	Voriconazole	70-82	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	15-19
31239195-14	2019	The FMO3 genotype altered the plasma exposure of voriconazole, while the CYP2C19 phenotype affected the metabolic capacity in immunocompromised patients.	Voriconazole	49-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-8
31401033-7	2019	Recombinant FMO3 proteins of the above and unanalyzed variants underwent kinetic analysis of their trimethylamine/benzydamine N-oxygenation activities.	trimethylamine	99-113	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-16
31401033-7	2019	Recombinant FMO3 proteins of the above and unanalyzed variants underwent kinetic analysis of their trimethylamine/benzydamine N-oxygenation activities.	benzydamine n	114-127	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-16
30351217-10	2019	These variant FMO3 proteins recombinantly expressed in Escherichia coli membranes exhibited decreased N-oxygenation activities toward trimethylamine (Vmax/Km < 40% that of the wild-type).	Nitrogen	102-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
30351217-10	2019	These variant FMO3 proteins recombinantly expressed in Escherichia coli membranes exhibited decreased N-oxygenation activities toward trimethylamine (Vmax/Km < 40% that of the wild-type).	trimethylamine	134-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
30351217-12	2019	Although the allele frequencies of the six new variants and/or haplotypes were low, the present results indicated that individuals homozygous or heterozygous for any of these novel missense FMO3 variants or known nonsense mutations such as p.(Cys197Ter) or p.(Arg205Cys) highly found in this self-reported Japanese trimethylaminuria cohort may have reduced FMO3 activity with respect to the N-oxygenation of trimethylamine.	trimethylamine	408-422	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	190-194
31405378-5	2019	RESULT: In this work, using benzydamine as a model drug, two easy-to-perform approaches (whole cell catalysis and enzyme immobilization) were investigated for the synthesis of FMO3-generated drug metabolites.	Benzydamine	28-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
30624777-10	2019	Further, we found that arecoline-induced H2AX expression was regulated by FMO3.	Arecoline	23-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	74-78
30982160-2	2019	Teneligliptin is a potent, selective, and long-lasting DPP-4 inhibitor with a t1/2 of approximately 24 h and unique pharmacokinetic properties: it is metabolized by cytochrome P450 (CYP) 3A4 and flavin-containing monooxygenase 3 (FMO3), or excreted from the kidney in an unchanged form.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	0-13	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	195-228
31295928-4	2019	Based on these studies, most of the vandetanib metabolism was attributed to N-desmethylvandetanib/vandetanib-N-oxide to CYP3A4/FMO3.	vandetanib	36-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-131
31295928-4	2019	Based on these studies, most of the vandetanib metabolism was attributed to N-desmethylvandetanib/vandetanib-N-oxide to CYP3A4/FMO3.	N-Desmethyl vandetanib	76-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-131
31295928-4	2019	Based on these studies, most of the vandetanib metabolism was attributed to N-desmethylvandetanib/vandetanib-N-oxide to CYP3A4/FMO3.	vandetanib	87-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-131
31295928-5	2019	Recombinant CYP3A4 was most efficient to form N-desmethylvandetanib, while FMO1/FMO3 generated N-oxide.	n-oxide	95-102	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
30982160-2	2019	Teneligliptin is a potent, selective, and long-lasting DPP-4 inhibitor with a t1/2 of approximately 24 h and unique pharmacokinetic properties: it is metabolized by cytochrome P450 (CYP) 3A4 and flavin-containing monooxygenase 3 (FMO3), or excreted from the kidney in an unchanged form.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	0-13	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	Choline	28-35	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-194
30690726-7	2019	Compared to the wild type, recombinant Lys158 -FMO3 and Gly308 -FMO3 variants significantly decreased the intrinsic clearance of ethionamide by 2% and 24%, respectively.	Ethionamide	129-140	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-68
30690726-8	2019	Two prevalent functional variants of FMO3 were predicted to affect ethionamide disposition, with mean ratios of Cmax and AUC of up to 1.5 and 1.7, respectively, in comparison with the wild type.	Ethionamide	67-78	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
30690726-9	2019	In comparing single ethionamide administration with the wild type, simulations of the combined effects of comedications and FMO3 genetic polymorphism estimated that the Cmax and AUC ratios of ethionamide increased up to 1.7 and 2.0, respectively.	Ethionamide	20-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	124-128
30690726-9	2019	In comparing single ethionamide administration with the wild type, simulations of the combined effects of comedications and FMO3 genetic polymorphism estimated that the Cmax and AUC ratios of ethionamide increased up to 1.7 and 2.0, respectively.	Ethionamide	192-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	124-128
30690726-10	2019	These findings suggested that FMO3-mediated drug-drug interaction and genetic polymorphism could be important determinants of interindividual heterogeneity in ethionamide disposition that need to be considered comprehensively to optimize the personalized dosing of ethionamide.	Ethionamide	159-170	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
30690726-10	2019	These findings suggested that FMO3-mediated drug-drug interaction and genetic polymorphism could be important determinants of interindividual heterogeneity in ethionamide disposition that need to be considered comprehensively to optimize the personalized dosing of ethionamide.	Ethionamide	265-276	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
30906589-1	2019	Flavin containing monooxygenase 3 [FMO3] encodes dimethylaniline monooxygenase [N-oxide-forming] 3, which breaks down nitrogen-containing compounds, and has been implicated in blood pressure regulation.	Nitrogen	118-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-33
30906589-1	2019	Flavin containing monooxygenase 3 [FMO3] encodes dimethylaniline monooxygenase [N-oxide-forming] 3, which breaks down nitrogen-containing compounds, and has been implicated in blood pressure regulation.	Nitrogen	118-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	35-39
30906589-1	2019	Flavin containing monooxygenase 3 [FMO3] encodes dimethylaniline monooxygenase [N-oxide-forming] 3, which breaks down nitrogen-containing compounds, and has been implicated in blood pressure regulation.	Nitrogen	118-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-98
30814476-4	2019	Human flavin-containing monooxygenase 3 (FMO3), which is the major hepatic enzyme involved in the production of N-oxide of trimethylamine, catalyzes the oxygenation of a variety of drug compounds.	n-oxide	112-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
30814476-4	2019	Human flavin-containing monooxygenase 3 (FMO3), which is the major hepatic enzyme involved in the production of N-oxide of trimethylamine, catalyzes the oxygenation of a variety of drug compounds.	n-oxide	112-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
30814476-4	2019	Human flavin-containing monooxygenase 3 (FMO3), which is the major hepatic enzyme involved in the production of N-oxide of trimethylamine, catalyzes the oxygenation of a variety of drug compounds.	trimethylamine	123-137	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
30814476-4	2019	Human flavin-containing monooxygenase 3 (FMO3), which is the major hepatic enzyme involved in the production of N-oxide of trimethylamine, catalyzes the oxygenation of a variety of drug compounds.	trimethylamine	123-137	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
29959872-0	2018	Flavin-Containing Monooxygenase 3 Polymorphic Variants Significantly Affect Clearance of Tamoxifen and Clomiphene.	Tamoxifen	89-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-33
29959872-0	2018	Flavin-Containing Monooxygenase 3 Polymorphic Variants Significantly Affect Clearance of Tamoxifen and Clomiphene.	Clomiphene	103-113	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-33
29959872-3	2018	The purpose of this study was to investigate the effect of the three common polymorphic variants of hFMO3 (V257M, E158K and E308G) on the metabolism and clearance of three structurally similar compounds: tamoxifen (breast cancer medication), clomiphene (infertility medication) and GSK5182 (antidiabetic lead molecule).	Tamoxifen	204-213	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
29959872-3	2018	The purpose of this study was to investigate the effect of the three common polymorphic variants of hFMO3 (V257M, E158K and E308G) on the metabolism and clearance of three structurally similar compounds: tamoxifen (breast cancer medication), clomiphene (infertility medication) and GSK5182 (antidiabetic lead molecule).	Clomiphene	242-252	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
29959872-3	2018	The purpose of this study was to investigate the effect of the three common polymorphic variants of hFMO3 (V257M, E158K and E308G) on the metabolism and clearance of three structurally similar compounds: tamoxifen (breast cancer medication), clomiphene (infertility medication) and GSK5182 (antidiabetic lead molecule).	GSK5182	282-289	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
30690726-0	2019	Physiologically Based Pharmacokinetic Modeling Approach to Predict Drug-Drug Interactions With Ethionamide Involving Impact of Genetic Polymorphism on FMO3.	Ethionamide	95-106	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	151-155
30690726-2	2019	We previously reported the major contribution of flavin-containing monooxygenase 3 (FMO3) in the reductive elimination pathway of ethionamide.	Ethionamide	130-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-82
30690726-2	2019	We previously reported the major contribution of flavin-containing monooxygenase 3 (FMO3) in the reductive elimination pathway of ethionamide.	Ethionamide	130-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	84-88
30690726-4	2019	The drug-drug interaction leading to methimazole affecting the disposition of ethionamide mediated by FMO3 was then quantitated using a bottom-up approach with a physiologically based pharmacokinetic framework.	Methimazole	37-48	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	102-106
30690726-4	2019	The drug-drug interaction leading to methimazole affecting the disposition of ethionamide mediated by FMO3 was then quantitated using a bottom-up approach with a physiologically based pharmacokinetic framework.	Ethionamide	78-89	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	102-106
30690726-7	2019	Compared to the wild type, recombinant Lys158 -FMO3 and Gly308 -FMO3 variants significantly decreased the intrinsic clearance of ethionamide by 2% and 24%, respectively.	Ethionamide	129-140	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
31240165-3	2019	Genetic testing, sequencing the entire coding region of the FMO3 gene has been recommended for affected individuals who convert less than 90% of the total TMA load to TMAO.	trimethyloxamine	167-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	60-64
30681159-8	2019	This mini review will provide a summary of the biochemical pathways, in which choline is involved and their respective inborn errors of metabolism (caused by mutations in SLC5A7, CHAT, SLC44A1, CHKB, PCYT1A, CEPT1, CAD; DHODH, UMPS, FMO3, DMGDH, and GNMT).	Choline	78-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	233-237
30420260-1	2019	Polymorphic human flavin-containing monooxygenase (FMO) 3 is an important drug-metabolizing enzyme for nitrogen- or sulfur-containing compounds.	Nitrogen	103-111	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-57
30420260-1	2019	Polymorphic human flavin-containing monooxygenase (FMO) 3 is an important drug-metabolizing enzyme for nitrogen- or sulfur-containing compounds.	Sulfur	116-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-57
30420260-7	2019	Seven variants showed substantially lower benzydamine N-oxygenation as compared with wild-type FMO3 protein.	Benzydamine	42-53	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-99
30420260-8	2019	Further analysis indicated that two of these variants, FMO3 G530A and R417H, showed significantly lower benzydamine N-oxygenation in liver microsomes of the homozygotes as compared with wild-type animals.	Benzydamine	104-115	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
30420260-8	2019	Further analysis indicated that two of these variants, FMO3 G530A and R417H, showed significantly lower benzydamine N-oxygenation in liver microsomes of the homozygotes as compared with wild-type animals.	Nitrogen	116-117	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	Choline	28-35	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	Carnitine	40-51	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-194
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	Carnitine	40-51	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethylamine	80-94	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-194
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethylamine	80-94	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethyloxamine	133-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-194
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethyloxamine	133-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethyloxamine	157-161	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-194
30347638-2	2018	Gut microbial metabolism of choline and l-carnitine results in the formation of trimethylamine (TMA) and concomitant conversion into trimethylamine-N-oxide (TMAO) by liver flavin monooxygenase 3 (FMO3).	trimethyloxamine	157-161	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
30347638-8	2018	FMO3 also impairs multiple aspects of cholesterol homeostasis, including transintestinal cholesterol export and macrophage-specific RCT.	Cholesterol	38-49	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
30347638-8	2018	FMO3 also impairs multiple aspects of cholesterol homeostasis, including transintestinal cholesterol export and macrophage-specific RCT.	Cholesterol	89-100	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
29353125-2	2018	TMAO levels show wide inter and intra individual variability in humans that can likely be accounted for by multiple factors including diet, the gut microbiota, levels of the TMAO generating liver enzyme Flavin-containing monooxygenase 3 (FMO3) and kidney function.	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-236
29959003-0	2018	Binding of methimazole and NADP(H) to human FMO3: In vitro and in silico studies.	Methimazole	11-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
29959003-0	2018	Binding of methimazole and NADP(H) to human FMO3: In vitro and in silico studies.	NADP	27-34	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
29959003-6	2018	Methimazole is a high-affinity substrate of hFMO3 and can competitively suppress the metabolism of other compounds.	Methimazole	0-11	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-49
29959003-7	2018	Our results demonstrate that methimazole Pi-stacks above the isoalloxazine ring of FAD in hFMO3, in a similar way to indole binding to the bacterial FMO.	Methimazole	29-40	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-95
29959003-7	2018	Our results demonstrate that methimazole Pi-stacks above the isoalloxazine ring of FAD in hFMO3, in a similar way to indole binding to the bacterial FMO.	isoalloxazine	61-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-95
29959003-7	2018	Our results demonstrate that methimazole Pi-stacks above the isoalloxazine ring of FAD in hFMO3, in a similar way to indole binding to the bacterial FMO.	indole	117-123	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-95
29959003-8	2018	However, for hFMO3 indole is found to act as a non-substrate competitive inhibitor.	indole	19-25	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	13-18
29959003-9	2018	Finally, understanding the binding mode of methimazole and indole could be advantageous for development of hFMO3 inhibitors, currently investigated as a possible treatment strategy for atherosclerosis.	Methimazole	43-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	107-112
29959003-9	2018	Finally, understanding the binding mode of methimazole and indole could be advantageous for development of hFMO3 inhibitors, currently investigated as a possible treatment strategy for atherosclerosis.	indole	59-65	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	107-112
29878384-0	2018	Development of a Physiologically Based Pharmacokinetic Model of Ethionamide in the Pediatric Population by Integrating Flavin-Containing Monooxygenase 3 Maturational Changes Over Time.	Ethionamide	64-75	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	119-152
29878384-5	2018	We hypothesized that the age-dependent changes in ethionamide elimination were predominantly a result of the progressive increases in the expression and metabolic capacity of FMO3 during childhood.	Ethionamide	50-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	175-179
29878384-7	2018	Thus, a good prediction PBPK model was validated successfully both in adults and children and applied to demonstrate the critical contribution of FMO3 in the mechanistic elimination pathway of ethionamide.	Ethionamide	193-204	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	146-150
29856598-11	2018	Nevertheless, the ubiquitous tissue expression of hmARC1 allows a continuous reduction of TMAO whereas the counter-reaction, the production of TMAO through FMO3, can take place only in the liver where FMO3 is expressed.	trimethyloxamine	143-147	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
29353125-2	2018	TMAO levels show wide inter and intra individual variability in humans that can likely be accounted for by multiple factors including diet, the gut microbiota, levels of the TMAO generating liver enzyme Flavin-containing monooxygenase 3 (FMO3) and kidney function.	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	238-242
29353125-2	2018	TMAO levels show wide inter and intra individual variability in humans that can likely be accounted for by multiple factors including diet, the gut microbiota, levels of the TMAO generating liver enzyme Flavin-containing monooxygenase 3 (FMO3) and kidney function.	trimethyloxamine	174-178	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	203-236
29353125-2	2018	TMAO levels show wide inter and intra individual variability in humans that can likely be accounted for by multiple factors including diet, the gut microbiota, levels of the TMAO generating liver enzyme Flavin-containing monooxygenase 3 (FMO3) and kidney function.	trimethyloxamine	174-178	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	238-242
29261803-0	2017	Correction: Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway.	Busulfan	61-70	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-45
28290528-0	2018	Nicotine dependence is associated with functional variation in FMO3, an enzyme that metabolizes nicotine in the brain.	Nicotine	0-8	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
28290528-0	2018	Nicotine dependence is associated with functional variation in FMO3, an enzyme that metabolizes nicotine in the brain.	Nicotine	96-104	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
28290528-1	2018	A common haplotype of the flavin-containing monooxygenase gene FMO3 is associated with aberrant mRNA splicing, a twofold reduction in in vivo nicotine N-oxidation and reduced nicotine dependence.	Nicotine	142-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
28290528-1	2018	A common haplotype of the flavin-containing monooxygenase gene FMO3 is associated with aberrant mRNA splicing, a twofold reduction in in vivo nicotine N-oxidation and reduced nicotine dependence.	Nicotine	175-183	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
28290528-4	2018	We determined the effects of common variants in FMO3 on plasma levels of nicotine-N-oxide in 170 European Americans administered deuterated nicotine.	nicotine 1-N-oxide	73-89	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
28290528-4	2018	We determined the effects of common variants in FMO3 on plasma levels of nicotine-N-oxide in 170 European Americans administered deuterated nicotine.	Nicotine	73-81	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
28290528-8	2018	As N-oxidation accounts for only a small percentage of hepatic nicotine metabolism we hypothesized that FMO3 genotype affects nicotine metabolism in the brain (unlike CYP2A6, FMO3 is expressed in human brain) or that nicotine-N-oxide itself has pharmacological activity.	Nicotine	126-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
28290528-9	2018	We demonstrate for the first time nicotine N-oxidation in human brain, mediated by FMO3 and FMO1, and show that nicotine-N-oxide modulates human alpha4beta2 nicotinic receptor activity in vitro.	Nicotine	34-42	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
29261803-0	2017	Correction: Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway.	Busulfan	61-70	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
29121650-0	2017	Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway.	Busulfan	49-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-33
29121650-0	2017	Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway.	Busulfan	49-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	35-39
29121650-7	2017	Furthermore, among different recombinant microsomal enzymes, the highest intrinsic clearance for THT was obtained via FMO3 followed by several CYPs including 2B6, 2C8, 2C9, 2C19, 2E1 and 3A4.	tetrahydrothiophene	97-100	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	118-122
29116146-3	2017	Certain mutations within the hFMO3 gene cause defective trimethylamine (TMA) N-oxygenation leading to trimethylaminuria (TMAU) also known as fish-odour syndrome.	trimethylamine	72-75	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-34
29121650-11	2017	Finally, in a Bu-treated patient, additional treatment with voriconazole (an antimycotic drug known as an FMO3-substrate) significantly altered the Bu clearance.	Busulfan	14-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
29121650-11	2017	Finally, in a Bu-treated patient, additional treatment with voriconazole (an antimycotic drug known as an FMO3-substrate) significantly altered the Bu clearance.	Voriconazole	60-72	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
29121650-12	2017	In conclusion, we demonstrate for the first time that FMO3 along with CYPs contribute a major part in busulphan metabolic pathway and certainly can affect its kinetics.	Busulfan	102-111	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
28724646-5	2017	The positive association between plasma TMAO and type 2 diabetes was consistent in each rs2266782 genotype group, and no significant interaction was observed (P = 0.093).Conclusions: Our results suggested that higher plasma TMAO was associated with increased odds of newly diagnosed type 2 diabetes and that this association was not modified by the FMO3 rs2266782 polymorphism.	trimethyloxamine	224-228	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	349-353
29116146-0	2017	Inactivation mechanism of N61S mutant of human FMO3 towards trimethylamine.	trimethylamine	60-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
29116146-3	2017	Certain mutations within the hFMO3 gene cause defective trimethylamine (TMA) N-oxygenation leading to trimethylaminuria (TMAU) also known as fish-odour syndrome.	trimethylamine	56-70	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-34
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Amphetamine	148-159	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Amphetamine	148-159	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Sulindac	161-169	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Sulindac	161-169	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Benzydamine	171-182	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Benzydamine	171-182	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Ranitidine	184-194	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Ranitidine	184-194	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Tamoxifen	196-205	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Tamoxifen	196-205	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Nicotine	207-215	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Nicotine	207-215	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Ethionamide	221-232	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Ethionamide	221-232	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Catecholamines	274-287	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	Catecholamines	274-287	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	trimethylamine	292-306	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-42
28819071-1	2017	Hepatic flavin-containing mono-oxygenase 3 (FMO3) metabolizes a broad array of nucleophilic heteroatom (e.g., N or S)-containing xenobiotics (e.g., amphetamine, sulindac, benzydamine, ranitidine, tamoxifen, nicotine, and ethionamide), as well as endogenous compounds (e.g., catecholamine and trimethylamine).	trimethylamine	292-306	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol	50-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
28255999-0	2017	Development of a physiologically based pharmacokinetic model to predict the effects of flavin-containing monooxygenase 3 (FMO3) polymorphisms on itopride exposure.	itopride	145-153	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-120
28255999-0	2017	Development of a physiologically based pharmacokinetic model to predict the effects of flavin-containing monooxygenase 3 (FMO3) polymorphisms on itopride exposure.	itopride	145-153	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	122-126
28255999-1	2017	Itopride, a substrate of FMO3, has been used for the symptomatic treatment of various gastrointestinal disorders.	itopride	0-8	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	25-29
28255999-2	2017	Physiologically based pharmacokinetic (PBPK) modeling was applied to evaluate the impact of FMO3 polymorphism on itopride pharmacokinetics (PK).	itopride	113-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	92-96
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol	50-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol	85-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol	85-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol	85-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol Esters	263-281	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
28872093-5	2017	TMAO poietin-monooxygenase 3 (FMO3) is a tool for cholesterol metabolism and reverse cholesterol transpor, lowering FMO3 can slow the gallbladder"s secretion of bile, delay intestinal absorption of cholesterol, and limit the synthesis of oxidized cholesterol and cholesterol esters.	Cholesterol Esters	263-281	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
28433924-8	2017	Notably, d9-TMAO and d9-trimethylamine were detected in skeletal muscle (n=6) at 6 h, and the enrichment ratio of d9-TMAO to d9-trimethylamine was influenced by a genetic variant in flavin-containing monooxygenase isoform 3 (FMO3 G472A).	d9-tmao	9-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	225-229
27943222-5	2017	Cediranib is metabolized via flavin-containing monooxygenase 1 and 3 (FMO1, FMO3) and uridine 5"-diphospho-glucuronosyltransferase (UGT) 1A4.	cediranib	0-9	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
28433924-8	2017	Notably, d9-TMAO and d9-trimethylamine were detected in skeletal muscle (n=6) at 6 h, and the enrichment ratio of d9-TMAO to d9-trimethylamine was influenced by a genetic variant in flavin-containing monooxygenase isoform 3 (FMO3 G472A).	d9-tmao	114-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	225-229
28433924-8	2017	Notably, d9-TMAO and d9-trimethylamine were detected in skeletal muscle (n=6) at 6 h, and the enrichment ratio of d9-TMAO to d9-trimethylamine was influenced by a genetic variant in flavin-containing monooxygenase isoform 3 (FMO3 G472A).	d9-trimethylamine	125-142	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	225-229
28433924-10	2017	TMAO exhibits fast turnover in the circulation with the majority being eliminated in urine within 24 h. A small portion of the dose, however, is taken up by extrahepatic tissue in a manner that appears to be under the influence of FMO3 G472A polymorphism.	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	231-235
28583088-10	2017	Finally, we found that liver-specific CHRNA4 transcription was highly correlated with genes involved in the nicotine metabolism, including CYP2A6, UGT2B7, and FMO3.	Nicotine	108-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	159-163
28413702-4	2017	Both FMO1 and FMO3 were potentially susceptible genes for nicotine metabolism process.	Nicotine	58-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
28084789-1	2017	AIM: In this paper, we developed a method to immobilize human flavin-containing monooxygenase-3 (hFMO3) using glutaraldehyde as a cross-linker onto amino-functionalized magnetic nanoparticles.	Glutaral	110-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-95
28114730-1	2017	The three-body fragment molecular orbital (FMO3) method is formulated for density-functional tight-binding (DFTB).	dftb	108-112	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-47
28114730-3	2017	The accuracy of FMO3-DFTB is evaluated for five proteins, sodium cation in explicit solvent, and three isomers of polyalanine.	dftb	21-25	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
28114730-3	2017	The accuracy of FMO3-DFTB is evaluated for five proteins, sodium cation in explicit solvent, and three isomers of polyalanine.	polyalanine	114-125	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
27837601-3	2017	This mini-review will focus on two such instances: the role of flavin-containing monooxygenase 3 (FMO3) in the formation of the cardiometabolic disease biomarker trimethylamine-N-oxide (TMAO) and the role of AhR as a sensor of endogenous ligands such as those generated by the gut microbiota.	trimethyloxamine	162-184	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-96
27837601-3	2017	This mini-review will focus on two such instances: the role of flavin-containing monooxygenase 3 (FMO3) in the formation of the cardiometabolic disease biomarker trimethylamine-N-oxide (TMAO) and the role of AhR as a sensor of endogenous ligands such as those generated by the gut microbiota.	trimethyloxamine	162-184	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	98-102
27837601-3	2017	This mini-review will focus on two such instances: the role of flavin-containing monooxygenase 3 (FMO3) in the formation of the cardiometabolic disease biomarker trimethylamine-N-oxide (TMAO) and the role of AhR as a sensor of endogenous ligands such as those generated by the gut microbiota.	trimethyloxamine	186-190	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-96
27837601-3	2017	This mini-review will focus on two such instances: the role of flavin-containing monooxygenase 3 (FMO3) in the formation of the cardiometabolic disease biomarker trimethylamine-N-oxide (TMAO) and the role of AhR as a sensor of endogenous ligands such as those generated by the gut microbiota.	trimethyloxamine	186-190	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	98-102
28196478-1	2017	BACKGROUND: Trimethylaminuria (TMAU) is a genetic disorder whereby people cannot convert trimethylamine (TMA) to its oxidized form (TMAO), a process that requires the liver enzyme FMO3.	Trimethylaminuria	12-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	180-184
28196478-1	2017	BACKGROUND: Trimethylaminuria (TMAU) is a genetic disorder whereby people cannot convert trimethylamine (TMA) to its oxidized form (TMAO), a process that requires the liver enzyme FMO3.	trimethylamine	89-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	180-184
28196478-1	2017	BACKGROUND: Trimethylaminuria (TMAU) is a genetic disorder whereby people cannot convert trimethylamine (TMA) to its oxidized form (TMAO), a process that requires the liver enzyme FMO3.	trimethylamine	31-34	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	180-184
28196478-1	2017	BACKGROUND: Trimethylaminuria (TMAU) is a genetic disorder whereby people cannot convert trimethylamine (TMA) to its oxidized form (TMAO), a process that requires the liver enzyme FMO3.	trimethyloxamine	132-136	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	180-184
28084789-3	2017	RESULTS: The apparent Km with clozapine as substrate and inhibition of hFMO3 by methimazole were explored for immobilized hFMO3 and were found to be comparable to literature values.	Clozapine	30-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	122-127
28084789-3	2017	RESULTS: The apparent Km with clozapine as substrate and inhibition of hFMO3 by methimazole were explored for immobilized hFMO3 and were found to be comparable to literature values.	Methimazole	80-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	71-76
28084789-3	2017	RESULTS: The apparent Km with clozapine as substrate and inhibition of hFMO3 by methimazole were explored for immobilized hFMO3 and were found to be comparable to literature values.	Methimazole	80-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	122-127
28084789-1	2017	AIM: In this paper, we developed a method to immobilize human flavin-containing monooxygenase-3 (hFMO3) using glutaraldehyde as a cross-linker onto amino-functionalized magnetic nanoparticles.	Glutaral	110-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-102
28084894-0	2017	Donors FMO3 polymorphisms affect tacrolimus elimination in Chinese liver transplant patients.	Tacrolimus	33-43	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-11
28084894-4	2017	RESULTS: Donor FMO3 rs1800822 allele T and rs909530 allele T were associated with fast tacrolimus elimination.	Tacrolimus	87-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	15-19
28084894-5	2017	Combination of polymorphisms of donor FMO3 rs1800822 and rs909530 genotype impacted on tacrolimus elimination (p = 0.0221).	Tacrolimus	87-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	38-42
28084894-7	2017	CONCLUSION: Donor"s FMO3 polymorphisms might affect tacrolimus elimination.	Tacrolimus	52-62	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	20-24
28331852-0	2017	Effects of FMO3 Polymorphisms on Pharmacokinetics of Sulindac in Chinese Healthy Male Volunteers.	Sulindac	53-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	11-15
28331852-6	2017	The mean values of Cmax, AUC0-24, and AUC0-  of sulindac were significantly higher in FMO3 hhdd group than those of FMO3 HHDD group (P < 0.05), while the pharmacokinetic parameters except Tmax of sulindac sulfide and sulindac sulfone showed no statistical difference between the two groups.	Sulindac	48-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	86-90
28331852-7	2017	The two FMO3 mutants were in close linkage disequilibrium and might play an important role in the pharmacokinetics of sulindac in Chinese healthy male volunteers.	Sulindac	118-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	8-12
26329789-5	2015	Consistent with previous reports, UGT1A4, CYP1A2, and flavin-containing monooxygenase 3 play major roles in catalyzing the formation of OLZ-10-N-glucuronide, 7-hydroxy-OLZ, and OLZ-N-oxide, respectively.	olz-10-n-glucuronide	136-156	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-87
27806989-0	2016	Correction to "Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease".	trimethylamine	15-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	60-93
27806989-0	2016	Correction to "Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease".	trimethylamine	15-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-99
27806989-0	2016	Correction to "Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease".	trimethyloxamine	34-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	60-93
27806989-0	2016	Correction to "Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease".	trimethyloxamine	34-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-99
27523475-1	2016	Human hepatic flavin-containing monooxygenase 3 (hFMO3) catalyses the monooxygenation of carbon-bound reactive heteroatoms and plays an important role in the metabolism of drugs and xenobiotics.	Carbon	89-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-47
27523475-1	2016	Human hepatic flavin-containing monooxygenase 3 (hFMO3) catalyses the monooxygenation of carbon-bound reactive heteroatoms and plays an important role in the metabolism of drugs and xenobiotics.	Carbon	89-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-54
27523475-5	2016	This was followed by structural mapping of 12 critical polymorphic variants and molecular docking experiments with five different known substrates/drugs of hFMO3 namely, benzydamine, sulindac sulfide, tozasertib, methimazole and trimethylamine.	Benzydamine	170-181	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-161
27523475-5	2016	This was followed by structural mapping of 12 critical polymorphic variants and molecular docking experiments with five different known substrates/drugs of hFMO3 namely, benzydamine, sulindac sulfide, tozasertib, methimazole and trimethylamine.	sulindac sulfide	183-199	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-161
27523475-5	2016	This was followed by structural mapping of 12 critical polymorphic variants and molecular docking experiments with five different known substrates/drugs of hFMO3 namely, benzydamine, sulindac sulfide, tozasertib, methimazole and trimethylamine.	VX680	201-211	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-161
27523475-5	2016	This was followed by structural mapping of 12 critical polymorphic variants and molecular docking experiments with five different known substrates/drugs of hFMO3 namely, benzydamine, sulindac sulfide, tozasertib, methimazole and trimethylamine.	trimethylamine	229-243	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-161
27523475-6	2016	Localisation of these mutations on the hFMO3 model provided a structural explanation for their observed biological effects and docked models of hFMO3-drug complexes gave insights into their binding mechanism demonstrating that nitrogen- and sulfur-containing substrates interact with the isoalloxazine ring through Pi-Cation interaction and Pi-Sulfur interactions, respectively.	Nitrogen	227-235	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-149
27523475-6	2016	Localisation of these mutations on the hFMO3 model provided a structural explanation for their observed biological effects and docked models of hFMO3-drug complexes gave insights into their binding mechanism demonstrating that nitrogen- and sulfur-containing substrates interact with the isoalloxazine ring through Pi-Cation interaction and Pi-Sulfur interactions, respectively.	Sulfur	241-247	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-149
27523475-6	2016	Localisation of these mutations on the hFMO3 model provided a structural explanation for their observed biological effects and docked models of hFMO3-drug complexes gave insights into their binding mechanism demonstrating that nitrogen- and sulfur-containing substrates interact with the isoalloxazine ring through Pi-Cation interaction and Pi-Sulfur interactions, respectively.	isoalloxazine	288-301	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	39-44
27523475-6	2016	Localisation of these mutations on the hFMO3 model provided a structural explanation for their observed biological effects and docked models of hFMO3-drug complexes gave insights into their binding mechanism demonstrating that nitrogen- and sulfur-containing substrates interact with the isoalloxazine ring through Pi-Cation interaction and Pi-Sulfur interactions, respectively.	isoalloxazine	288-301	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-149
27523475-6	2016	Localisation of these mutations on the hFMO3 model provided a structural explanation for their observed biological effects and docked models of hFMO3-drug complexes gave insights into their binding mechanism demonstrating that nitrogen- and sulfur-containing substrates interact with the isoalloxazine ring through Pi-Cation interaction and Pi-Sulfur interactions, respectively.	Sulfur	344-350	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-149
27320963-0	2016	What is the contribution of human FMO3 in the N-oxygenation of selected therapeutic drugs and drugs of abuse?	Nitrogen	46-47	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
27320963-3	2016	The aim of the presented study was to elucidate the contribution of human FMO3 to the N-oxygenation of selected therapeutic drugs and drugs of abuse (DOAs).	Nitrogen	86-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	74-78
27320963-7	2016	FMO3 was identified as enzyme mainly responsible for the formation of N,N-diallyltryptamine N-oxide and methamphetamine hydroxylamine (>80% contribution for both).	n,n-diallyltryptamine n-oxide	70-99	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
27320963-7	2016	FMO3 was identified as enzyme mainly responsible for the formation of N,N-diallyltryptamine N-oxide and methamphetamine hydroxylamine (>80% contribution for both).	methamphetamine hydroxylamine	104-133	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
27320963-9	2016	However, FMO3 contributed with less than 5% to the formation of 3-bromomethcathinone hydroxylamine, amitriptyline N-oxide, and clozapine N-oxide.	3-bromomethcathinone hydroxylamine	64-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
27320963-9	2016	However, FMO3 contributed with less than 5% to the formation of 3-bromomethcathinone hydroxylamine, amitriptyline N-oxide, and clozapine N-oxide.	amitriptyline N-oxide	100-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
27320963-9	2016	However, FMO3 contributed with less than 5% to the formation of 3-bromomethcathinone hydroxylamine, amitriptyline N-oxide, and clozapine N-oxide.	clozapine N-oxide	127-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
27513517-0	2016	Association of FMO3 Variants and Trimethylamine N-Oxide Concentration, Disease Progression, and Mortality in CKD Patients.	trimethyloxamine	33-55	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	15-19
27513517-2	2016	TMAO is generated from trimethylamine (TMA) via metabolism by hepatic flavin-containing monooxygenase isoform 3 (FMO3).	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-111
27513517-2	2016	TMAO is generated from trimethylamine (TMA) via metabolism by hepatic flavin-containing monooxygenase isoform 3 (FMO3).	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-117
27513517-2	2016	TMAO is generated from trimethylamine (TMA) via metabolism by hepatic flavin-containing monooxygenase isoform 3 (FMO3).	trimethylamine	23-37	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-111
27513517-2	2016	TMAO is generated from trimethylamine (TMA) via metabolism by hepatic flavin-containing monooxygenase isoform 3 (FMO3).	trimethylamine	23-37	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-117
27513517-3	2016	We determined the functional effects of three common FMO3 variants at amino acids 158, 308, and 257 on TMAO concentrations in a prospective cohort study and evaluated associations of polymorphisms with CKD progression and mortality.	trimethyloxamine	103-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	53-57
27190056-0	2016	Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease.	trimethylamine	0-14	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	45-78
27190056-0	2016	Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease.	trimethylamine	0-14	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
27190056-0	2016	Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease.	trimethyloxamine	19-41	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	45-78
27190056-0	2016	Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease.	trimethyloxamine	19-41	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
27190056-3	2016	FMO3 converts the odorous TMA to nonodorous TMA N-oxide (TMAO), which is excreted in urine.	trimethylamine	26-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
27190056-3	2016	FMO3 converts the odorous TMA to nonodorous TMA N-oxide (TMAO), which is excreted in urine.	trimethyloxamine	44-55	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
27190056-3	2016	FMO3 converts the odorous TMA to nonodorous TMA N-oxide (TMAO), which is excreted in urine.	trimethyloxamine	57-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
27190056-4	2016	Impaired FMO3 activity gives rise to the inherited disorder primary trimethylaminuria (TMAU).	Trimethylaminuria	87-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
27190056-7	2016	Recently, there has been much interest in FMO3 and its catalytic product, TMAO, because TMAO has been implicated in various conditions affecting health, including cardiovascular disease, reverse cholesterol transport, and glucose and lipid homeostasis.	trimethyloxamine	74-78	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
27190056-7	2016	Recently, there has been much interest in FMO3 and its catalytic product, TMAO, because TMAO has been implicated in various conditions affecting health, including cardiovascular disease, reverse cholesterol transport, and glucose and lipid homeostasis.	trimethyloxamine	88-92	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
27190056-7	2016	Recently, there has been much interest in FMO3 and its catalytic product, TMAO, because TMAO has been implicated in various conditions affecting health, including cardiovascular disease, reverse cholesterol transport, and glucose and lipid homeostasis.	Cholesterol	195-206	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
27190056-7	2016	Recently, there has been much interest in FMO3 and its catalytic product, TMAO, because TMAO has been implicated in various conditions affecting health, including cardiovascular disease, reverse cholesterol transport, and glucose and lipid homeostasis.	Glucose	222-229	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
26856397-1	2016	OBJECTIVE: The antipsychotic olanzapine is reportedly metabolized by inducible human cytochrome P450 (CYP) 1A2 and variable copy-number CYP2D6 and polymorphic flavin-containing monooxygenase 3 (FMO3) in different pathways.	Olanzapine	29-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	159-192
26856397-1	2016	OBJECTIVE: The antipsychotic olanzapine is reportedly metabolized by inducible human cytochrome P450 (CYP) 1A2 and variable copy-number CYP2D6 and polymorphic flavin-containing monooxygenase 3 (FMO3) in different pathways.	Olanzapine	29-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	194-198
26856397-4	2016	RESULTS: Furafylline (a CYP1A2 inhibitor), quinidine (a CYP2D6 inhibitor), and heat treatment (inactivates FMO3) suppressed liver microsomal metabolic clearance of olanzapine by approximately 30%.	Olanzapine	164-174	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	107-111
26856397-5	2016	Olanzapine N-demethylation and N-oxygenation were found to be catalyzed by CYP1A2 and CYP2D6 and by CYP2D6 and FMO3, respectively, in experiments using liver microsomes and recombinant enzymes.	Olanzapine	0-10	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	111-115
26856397-5	2016	Olanzapine N-demethylation and N-oxygenation were found to be catalyzed by CYP1A2 and CYP2D6 and by CYP2D6 and FMO3, respectively, in experiments using liver microsomes and recombinant enzymes.	Nitrogen	11-12	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	111-115
28649550-9	2015	These variant FMO3 proteins recombinantly expressed in Escherichia coli membranes exhibited decreased N-oxygenation activities toward trimethylamine and benzydamine.	Nitrogen	102-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
28649550-9	2015	These variant FMO3 proteins recombinantly expressed in Escherichia coli membranes exhibited decreased N-oxygenation activities toward trimethylamine and benzydamine.	trimethylamine	134-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
28649550-9	2015	These variant FMO3 proteins recombinantly expressed in Escherichia coli membranes exhibited decreased N-oxygenation activities toward trimethylamine and benzydamine.	Benzydamine	153-164	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	14-18
26329789-5	2015	Consistent with previous reports, UGT1A4, CYP1A2, and flavin-containing monooxygenase 3 play major roles in catalyzing the formation of OLZ-10-N-glucuronide, 7-hydroxy-OLZ, and OLZ-N-oxide, respectively.	7-hydroxy-olz	158-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-87
26329789-5	2015	Consistent with previous reports, UGT1A4, CYP1A2, and flavin-containing monooxygenase 3 play major roles in catalyzing the formation of OLZ-10-N-glucuronide, 7-hydroxy-OLZ, and OLZ-N-oxide, respectively.	olz-n-oxide	177-188	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-87
25630629-0	2015	Human flavin-containing monooxygenase 3 on graphene oxide for drug metabolism screening.	graphene oxide	43-57	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
26496755-4	2015	Moreover, sgRNA targeting flavin containing monooxygenases3 (Fmo3) gene and the corresponding single strand oligonucleotides (ssODN) donor template with point mutation were co-injected into the male pronucleus of one-cell mouse embryos stimulated HR-mediated repair mechanism.	4,6-dinitro-o-cresol	26-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
26666012-3	2015	Several studies indicated that variability in the expression of FMO3 involved in some nitrogen, or sulfur-containing durg metabolism.	Nitrogen	86-94	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-68
26666012-3	2015	Several studies indicated that variability in the expression of FMO3 involved in some nitrogen, or sulfur-containing durg metabolism.	Sulfur	99-105	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-68
26666012-3	2015	Several studies indicated that variability in the expression of FMO3 involved in some nitrogen, or sulfur-containing durg metabolism.	durg	117-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-68
25451157-7	2015	GSK5182 N-demethylation and hydroxylation is mainly mediated by CYP3A4, whereas FMO1 and FMO3 contribute to the formation of GSK5182 N-oxide from GSK5182.	gsk5182 n-oxide	125-140	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-93
25630629-1	2015	Human flavin-containing monooxygenase 3 (hFMO3), a membrane-bound hepatic protein, belonging to the second most important class of phase-1 drug-metabolizing enzymes, was immobilized in its active form on graphene oxide (GO) for enhanced electrochemical response.	graphene oxide	204-218	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
25630629-1	2015	Human flavin-containing monooxygenase 3 (hFMO3), a membrane-bound hepatic protein, belonging to the second most important class of phase-1 drug-metabolizing enzymes, was immobilized in its active form on graphene oxide (GO) for enhanced electrochemical response.	graphene oxide	204-218	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
25630629-1	2015	Human flavin-containing monooxygenase 3 (hFMO3), a membrane-bound hepatic protein, belonging to the second most important class of phase-1 drug-metabolizing enzymes, was immobilized in its active form on graphene oxide (GO) for enhanced electrochemical response.	graphene oxide	220-222	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
25630629-1	2015	Human flavin-containing monooxygenase 3 (hFMO3), a membrane-bound hepatic protein, belonging to the second most important class of phase-1 drug-metabolizing enzymes, was immobilized in its active form on graphene oxide (GO) for enhanced electrochemical response.	graphene oxide	220-222	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
25630629-2	2015	To improve protein stabilization and to ensure the electrocatalytic activity of the immobilized enzyme, didodecyldimethylammonium bromide (DDAB) was used to mimic lipid layers of biological membranes and acted as an interface between GO nanomaterial and the hFMO3 biocomponent.	didodecyldimethylammonium	104-137	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	258-263
25630629-2	2015	To improve protein stabilization and to ensure the electrocatalytic activity of the immobilized enzyme, didodecyldimethylammonium bromide (DDAB) was used to mimic lipid layers of biological membranes and acted as an interface between GO nanomaterial and the hFMO3 biocomponent.	didodecyldimethylammonium	139-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	258-263
25460299-3	2014	FMO3 mutations have been associated with the incidence and severity of trimethylaminuria (TMAU), a metabolic disorder characterized by the inability of the affected individual to metabolize the odorous trimethylamine to its non-odorous N-oxide.	trimethylamine	202-216	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
25760531-6	2015	High benzydamine N-oxygenation activities of recombinant human FMO1 and FMO3 and human kidney microsomes were observed at pH 8.4, whereas N-demethylation by cytochrome P450 2D6 was faster at pH 7.4.	benzydamine n	5-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
25760531-6	2015	High benzydamine N-oxygenation activities of recombinant human FMO1 and FMO3 and human kidney microsomes were observed at pH 8.4, whereas N-demethylation by cytochrome P450 2D6 was faster at pH 7.4.	Nitrogen	17-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
25760532-1	2015	Human flavin-containing monooxygenase 3 (FMO3) in the liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Nitrogen	99-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
25760532-1	2015	Human flavin-containing monooxygenase 3 (FMO3) in the liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Nitrogen	99-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
25760532-1	2015	Human flavin-containing monooxygenase 3 (FMO3) in the liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Sulfur	113-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
25760532-1	2015	Human flavin-containing monooxygenase 3 (FMO3) in the liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Sulfur	113-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
25760532-2	2015	Because of growing interest in drug interactions mediated by polymorphic FMO3, benzydamine N-oxygenation by human FMO3 was investigated as a model reaction.	benzydamine n	79-92	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
25760532-2	2015	Because of growing interest in drug interactions mediated by polymorphic FMO3, benzydamine N-oxygenation by human FMO3 was investigated as a model reaction.	benzydamine n	79-92	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	114-118
25760532-5	2015	Apparent competitive inhibition by methimazole (0-50 muM) of sulindac sulfide S-oxygenation was observed with FMO3 proteins.	Methimazole	35-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	110-114
25760532-5	2015	Apparent competitive inhibition by methimazole (0-50 muM) of sulindac sulfide S-oxygenation was observed with FMO3 proteins.	sulindac sulfide	61-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	110-114
25760532-6	2015	Sulindac sulfide S-oxygenation activity of Arg205Cys variant FMO3 protein was likely to be suppressed more by methimazole than wild-type or Val257Met variant FMO3 protein was.	sulindac sulfide	0-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
25760532-6	2015	Sulindac sulfide S-oxygenation activity of Arg205Cys variant FMO3 protein was likely to be suppressed more by methimazole than wild-type or Val257Met variant FMO3 protein was.	sulindac sulfide	0-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	158-162
25760532-6	2015	Sulindac sulfide S-oxygenation activity of Arg205Cys variant FMO3 protein was likely to be suppressed more by methimazole than wild-type or Val257Met variant FMO3 protein was.	Methimazole	110-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
25760532-7	2015	These results suggest that genetic polymorphism in the human FMO3 gene may lead to changes of drug interactions for N- or S-oxygenations of xenobiotics and endogenous substances and that a probe battery system of benzydamine N-oxygenation and sulindac sulfide S-oxygenation activities is recommended to clarify the drug interactions mediated by FMO3.	benzydamine n	213-226	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
25760532-7	2015	These results suggest that genetic polymorphism in the human FMO3 gene may lead to changes of drug interactions for N- or S-oxygenations of xenobiotics and endogenous substances and that a probe battery system of benzydamine N-oxygenation and sulindac sulfide S-oxygenation activities is recommended to clarify the drug interactions mediated by FMO3.	sulindac sulfide	243-259	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
25378658-6	2015	In vivo and in vitro results were consistent with the concept that the effects were mediated directly by FMO3 rather than trimethylamine/TMAO; in particular, overexpression of FMO3 in the human hepatoma cell line, Hep3B, resulted in significantly increased glucose secretion and lipogenesis.	Glucose	257-264	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
25460299-3	2014	FMO3 mutations have been associated with the incidence and severity of trimethylaminuria (TMAU), a metabolic disorder characterized by the inability of the affected individual to metabolize the odorous trimethylamine to its non-odorous N-oxide.	n-oxide	236-243	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
25460299-4	2014	In addition to this primary genetic form, there are other forms of TMAU that support the hypothesis that FMO3 activity may be modulated by steroid hormones.	Steroids	139-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	105-109
25460299-5	2014	To understand the molecular mechanism involved in the regulation of Fmo3 gene expression by steroid hormones, we performed this study in an in vitro cellular system, mouse liver cells, and on the human FMO3 gene.	Steroids	92-108	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	202-206
25460299-7	2014	The use of increased concentration of theophylline inhibited estrogen receptor alpha (ERalpha)-mediated transcription of Fmo3 mRNA.	Theophylline	38-50	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	121-125
25460299-8	2014	17beta-Estradiol inhibited Fmo3 mRNA accumulation.	Estradiol	0-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
25460299-15	2014	Thus, 17beta-estradiol plays a fundamental role in the regulation of Fmo3 gene transcription.	Estradiol	6-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	69-73
24165757-3	2014	This study explored the association between the CYP2C9, CYP2C19, CYP2B6 and FMO3 genotypes and sulfolane (Su, a water soluble metabolite of Bu) plasma levels in children undergoing hematopoietic stem cell transplantation (HSCT).	sulfolane	95-104	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
25224784-0	2014	Effect of two-linked mutations of the FMO3 gene on itopride metabolism in Chinese healthy volunteers.	itopride	51-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	38-42
25224784-2	2014	Flavin-containing monooxygenase 3 (FMO3) has been confirmed to be the key enzyme involved in the main itopride metabolic pathway.	itopride	102-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-33
25224784-2	2014	Flavin-containing monooxygenase 3 (FMO3) has been confirmed to be the key enzyme involved in the main itopride metabolic pathway.	itopride	102-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	35-39
25224784-3	2014	We investigated whether the FMO3 genotypes can affect itopride metabolism in Chinese healthy volunteers.	itopride	54-62	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	28-32
25224784-6	2014	RESULTS: Itopride and itopride N-oxide both exhibit FMO3 genotype-dependent pharmacokinetic profiles.	itopride	9-17	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	52-56
25224784-6	2014	RESULTS: Itopride and itopride N-oxide both exhibit FMO3 genotype-dependent pharmacokinetic profiles.	itopride	22-30	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	52-56
25224784-6	2014	RESULTS: Itopride and itopride N-oxide both exhibit FMO3 genotype-dependent pharmacokinetic profiles.	n-oxide	31-38	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	52-56
25224784-10	2014	CONCLUSION: The FMO3 allele can significantly affect the metabolism of itopride.	itopride	71-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
25119182-14	2014	FMO3-H1/H3 genotype was associated with lower daunorubicin clearance than FMO3-H1/H1, p = 0.00829.	Daunorubicin	46-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
25119182-18	2014	We found suggestive associations between FMO3 and GSTP1 haplotypes with daunorubicin PK that could potentially affect efficacy and toxicity.	Daunorubicin	72-84	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
25288227-1	2014	INTRODUCTION: Trimethylaminuria is a rare inherited disorder due to decreased metabolism of dietary-derived trimethylamine by flavin-containing monooxygenase 3.	trimethylamine	108-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	126-159
25288227-2	2014	Several single nucleotide polymorphisms of the flavin-containing monooxygenase 3 gene have been described and result in an enzyme with decreased or abolished functional activity for trimethylamine N-oxygenation thus leading to trimethylaminuria.	trimethylamine	182-196	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-80
25271725-2	2014	A meta-organismal pathway was elucidated involving gut microbiota-dependent formation of TMA and host hepatic flavin monooxygenase 3-dependent (FMO3-dependent) formation of TMA-N-oxide (TMAO), a metabolite shown to be both mechanistically linked to atherosclerosis and whose levels are strongly linked to cardiovascular disease (CVD) risks.	trimethyloxamine	173-184	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-148
25271725-2	2014	A meta-organismal pathway was elucidated involving gut microbiota-dependent formation of TMA and host hepatic flavin monooxygenase 3-dependent (FMO3-dependent) formation of TMA-N-oxide (TMAO), a metabolite shown to be both mechanistically linked to atherosclerosis and whose levels are strongly linked to cardiovascular disease (CVD) risks.	trimethyloxamine	186-190	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-148
24727368-9	2014	The majority of thiones were poor substrates for hFMO3, the major form in adult human liver.	Thiones	16-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-54
23797843-4	2014	Targeted LC-MS/MS analysis of hepatocyte incubations using chemical inhibitors indicated that PQ was predominantly metabolized by CYPs 3A4, 1A2 and 2D6, MAO-A, -B and FMO-3.	Primaquine	94-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	167-172
24165757-3	2014	This study explored the association between the CYP2C9, CYP2C19, CYP2B6 and FMO3 genotypes and sulfolane (Su, a water soluble metabolite of Bu) plasma levels in children undergoing hematopoietic stem cell transplantation (HSCT).	sulfolane	106-108	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
24028545-1	2014	AIM: The aim of this study was to investigate relationships between flavin-containing mono-oxygenase 3 (FMO3) genotype and phenotype (conversion of odorous trimethylamine into non-odorous trimethylamine N-oxide) in a large Japanese cohort suffering from trimethylaminuria.	trimethyloxamine	188-210	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
24028545-7	2014	Twenty-seven mutations were identified in FMO3, 15 in the coding region, of which eight abolish or severely impair FMO3 activity (Pro70Leu, Cys197fsX, Thr201Lys, Arg205Cys, Met260Val, Trp388Ter, Gln470Ter and Arg500Ter), and 12 in the upstream region.	cys197fsx	140-149	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
24028545-1	2014	AIM: The aim of this study was to investigate relationships between flavin-containing mono-oxygenase 3 (FMO3) genotype and phenotype (conversion of odorous trimethylamine into non-odorous trimethylamine N-oxide) in a large Japanese cohort suffering from trimethylaminuria.	trimethylamine	156-170	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-102
24028545-1	2014	AIM: The aim of this study was to investigate relationships between flavin-containing mono-oxygenase 3 (FMO3) genotype and phenotype (conversion of odorous trimethylamine into non-odorous trimethylamine N-oxide) in a large Japanese cohort suffering from trimethylaminuria.	trimethylamine	156-170	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
24028545-1	2014	AIM: The aim of this study was to investigate relationships between flavin-containing mono-oxygenase 3 (FMO3) genotype and phenotype (conversion of odorous trimethylamine into non-odorous trimethylamine N-oxide) in a large Japanese cohort suffering from trimethylaminuria.	trimethyloxamine	188-210	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-102
24028545-7	2014	Twenty-seven mutations were identified in FMO3, 15 in the coding region, of which eight abolish or severely impair FMO3 activity (Pro70Leu, Cys197fsX, Thr201Lys, Arg205Cys, Met260Val, Trp388Ter, Gln470Ter and Arg500Ter), and 12 in the upstream region.	trp388ter	184-193	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
24028545-7	2014	Twenty-seven mutations were identified in FMO3, 15 in the coding region, of which eight abolish or severely impair FMO3 activity (Pro70Leu, Cys197fsX, Thr201Lys, Arg205Cys, Met260Val, Trp388Ter, Gln470Ter and Arg500Ter), and 12 in the upstream region.	gln470ter	195-204	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
23855261-10	2014	CYP3A4 and FMO3 are the major enzymes responsible for the metabolism of teneligliptin in humans.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	72-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	11-15
24448396-0	2014	Variation in P450 oxidoreductase (POR) A503V and flavin-containing monooxygenase (FMO)-3 E158K is associated with minor alterations in nicotine metabolism, but does not alter cigarette consumption.	Nicotine	135-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-88
24448396-4	2014	In 130 nonsmokers of African descent who received 4 mg oral nicotine, FMO3 158K trended toward slower nicotine metabolism in reduced CYP2A6 metabolizers (P=0.07) only, whereas POR 503V was associated with faster CYP2A6 activity (nicotine metabolite ratio) in normal (P=0.03), but not reduced, CYP2A6 metabolizers.	Nicotine	60-68	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
24448396-4	2014	In 130 nonsmokers of African descent who received 4 mg oral nicotine, FMO3 158K trended toward slower nicotine metabolism in reduced CYP2A6 metabolizers (P=0.07) only, whereas POR 503V was associated with faster CYP2A6 activity (nicotine metabolite ratio) in normal (P=0.03), but not reduced, CYP2A6 metabolizers.	Nicotine	102-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
24448396-4	2014	In 130 nonsmokers of African descent who received 4 mg oral nicotine, FMO3 158K trended toward slower nicotine metabolism in reduced CYP2A6 metabolizers (P=0.07) only, whereas POR 503V was associated with faster CYP2A6 activity (nicotine metabolite ratio) in normal (P=0.03), but not reduced, CYP2A6 metabolizers.	Nicotine	102-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
24448396-6	2014	Thus, FMO3 E158K and POR A503V are minor sources of nicotine metabolism variation, insufficient to appreciably alter smoking.	Nicotine	52-60	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
24173915-0	2014	Effects of single-nucleotide polymorphisms of FMO3 and FMO6 genes on pharmacokinetic characteristics of sulindac sulfide in premature labor.	sulindac sulfide	104-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
24173915-1	2014	This study aimed to investigate the effects of polymorphisms of the flavin-containing mono-oxygenase 3 (FMO3) and flavin-containing mono-oxygenase 6 (FMO6) genes on the pharmacokinetics of sulindac sulfide, the active metabolite of sulindac, in patients with preterm labor.	sulindac sulfide	189-205	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-102
23821320-2	2014	The condition is caused by deficiency of flavin-containing monooxygenase 3 (FMO3) which leads to impairment of hepatic TMA oxidation to the odorless trimethylamine N-oxide.	trimethyloxamine	149-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-74
24173915-1	2014	This study aimed to investigate the effects of polymorphisms of the flavin-containing mono-oxygenase 3 (FMO3) and flavin-containing mono-oxygenase 6 (FMO6) genes on the pharmacokinetics of sulindac sulfide, the active metabolite of sulindac, in patients with preterm labor.	sulindac sulfide	189-205	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
24173915-1	2014	This study aimed to investigate the effects of polymorphisms of the flavin-containing mono-oxygenase 3 (FMO3) and flavin-containing mono-oxygenase 6 (FMO6) genes on the pharmacokinetics of sulindac sulfide, the active metabolite of sulindac, in patients with preterm labor.	Sulindac	189-197	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-102
24173915-1	2014	This study aimed to investigate the effects of polymorphisms of the flavin-containing mono-oxygenase 3 (FMO3) and flavin-containing mono-oxygenase 6 (FMO6) genes on the pharmacokinetics of sulindac sulfide, the active metabolite of sulindac, in patients with preterm labor.	Sulindac	189-197	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
24173915-4	2014	The AUC(last) of sulindac sulfide was significantly higher in patients with variant-type homozygotes of FMO3 (rs909530) than those with ancestral alleles or heterozygotes.	sulindac sulfide	17-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
24173915-6	2014	From multiple linear regression models, FMO3 (rs909530) was found to have significant influence on the AUClast of sulindac sulfide after adjusting for gestational age, weight, and all studied SNPs.	sulindac sulfide	114-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
23821320-2	2014	The condition is caused by deficiency of flavin-containing monooxygenase 3 (FMO3) which leads to impairment of hepatic TMA oxidation to the odorless trimethylamine N-oxide.	trimethyloxamine	149-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
23930678-6	2013	The formation of the various olanzapine metabolites is influenced by polymorphisms in the genes coding for CYP1A2, CYP1A expression regulator AHR, UGT1A4 and UGT2B10, as well as FMO3.	Olanzapine	29-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	178-182
23791655-1	2013	Trimethylaminuria (TMAu) or "fish odor syndrome" is a metabolic disorder characterized by the inability to convert malodorous dietarily-derived trimethylamine (TMA) to odorless TMA N-oxide by the flavin-containing monooxygenase 3 (FMO3).	Trimethylaminuria	19-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	231-235
23791655-1	2013	Trimethylaminuria (TMAu) or "fish odor syndrome" is a metabolic disorder characterized by the inability to convert malodorous dietarily-derived trimethylamine (TMA) to odorless TMA N-oxide by the flavin-containing monooxygenase 3 (FMO3).	trimethylamine	19-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	231-235
23147717-5	2013	The influence of FMO3 polymorphisms was limited to variability in OLA N-oxide.	Olanzapine	66-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	17-21
23147717-5	2013	The influence of FMO3 polymorphisms was limited to variability in OLA N-oxide.	n-oxide	70-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	17-21
23147717-7	2013	Our data support the role of FMO3 in the N-oxidation of OLA and implicate for the first time the contribution of FMO1 and its functional *6 variant in OLA disposition.	Olanzapine	56-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-33
23640382-6	2013	The reverse was observed for the formation of DMANO by FMO3.	dmano	46-51	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
24028108-6	2013	The results show that delocalized electronic orbitals with covalent and hydrogen bonds are better described at the trimer level, and the FMO3-LCMO method is applicable to quantitative evaluations of a wide range of frontier orbitals in large biosystems.	Hydrogen	72-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
23567996-1	2013	Human flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) in liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Nitrogen	109-117	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
23758476-5	2013	We found that 12 SNPs in seven genes (ABCC6, ABCG1, ABCG2, CYP1A2, CYP2D6, FMO2, and FMO3) were significantly associated with febrile neutropenia after docetaxel treatment.	Docetaxel	152-161	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	85-89
23567996-2	2013	Loss-of-function mutations of the FMO3 gene, the enzyme responsible for trimethylamine N-oxygenation, cause the inherited disorder trimethylaminuria (also known as fish odor syndrome).	trimethylamine n	72-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
23567996-4	2013	Then, the activities of FMO3 variants in human liver microsomes and the activities of recombinantly expressed FMO3 variant proteins with respect to the oxygenation of nitrogen- and sulfur-containing drugs were summarized and the potential for drug interactions was demonstrated.	Nitrogen	167-175	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	110-114
23567996-4	2013	Then, the activities of FMO3 variants in human liver microsomes and the activities of recombinantly expressed FMO3 variant proteins with respect to the oxygenation of nitrogen- and sulfur-containing drugs were summarized and the potential for drug interactions was demonstrated.	Sulfur	181-187	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	110-114
23567996-1	2013	Human flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) in liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Nitrogen	109-117	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
23567996-1	2013	Human flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) in liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Sulfur	123-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
23567996-1	2013	Human flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) in liver catalyzes a variety of oxygenations of nitrogen- and sulfur-containing medicines and xenobiotic substances.	Sulfur	123-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
23656565-4	2013	Dietary carnitine (present predominately in red meat) and lecithin (phosphatidyl choline) are shown to be metabolized by gut microbes to trimethylamine (TMA), which in turn is metabolized by liver flavin monoxygenases (especially FMO3 and FMO1) to form trimethylamine-N-oxide (TMAO).	Carnitine	8-17	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
23656565-4	2013	Dietary carnitine (present predominately in red meat) and lecithin (phosphatidyl choline) are shown to be metabolized by gut microbes to trimethylamine (TMA), which in turn is metabolized by liver flavin monoxygenases (especially FMO3 and FMO1) to form trimethylamine-N-oxide (TMAO).	Lecithins	58-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
23656565-4	2013	Dietary carnitine (present predominately in red meat) and lecithin (phosphatidyl choline) are shown to be metabolized by gut microbes to trimethylamine (TMA), which in turn is metabolized by liver flavin monoxygenases (especially FMO3 and FMO1) to form trimethylamine-N-oxide (TMAO).	Phosphatidylcholines	68-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
23656565-4	2013	Dietary carnitine (present predominately in red meat) and lecithin (phosphatidyl choline) are shown to be metabolized by gut microbes to trimethylamine (TMA), which in turn is metabolized by liver flavin monoxygenases (especially FMO3 and FMO1) to form trimethylamine-N-oxide (TMAO).	trimethylamine	137-151	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
23266626-1	2013	The N-oxygenation of amines by the human flavin-containing monooxygenase (form 3) (FMO3) represents an important means for the conversion of lipophilic nucleophilic heteroatom-containing compounds into more polar and readily excreted products.	Amines	21-27	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-81
23266626-1	2013	The N-oxygenation of amines by the human flavin-containing monooxygenase (form 3) (FMO3) represents an important means for the conversion of lipophilic nucleophilic heteroatom-containing compounds into more polar and readily excreted products.	Amines	21-27	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
23266626-3	2013	Several single nucleotide polymorphisms (SNPs) of the FMO3 gene have been described and result in an enzyme with decreased or abolished functional activity for TMA N-oxygenation thus leading to TMAU, or fish-like odor syndrome.	trimethylamine	160-163	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
23266626-3	2013	Several single nucleotide polymorphisms (SNPs) of the FMO3 gene have been described and result in an enzyme with decreased or abolished functional activity for TMA N-oxygenation thus leading to TMAU, or fish-like odor syndrome.	Trimethylaminuria	194-198	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
23266626-12	2013	Urinary determination of TMA/TMAO ratio in 158KK/308EG individuals showed a considerable reduction in FMO3 activity although they do not show the classical features of trimethylaminuria as a strong body odor and breath.	trimethylamine	25-28	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	102-106
23266626-12	2013	Urinary determination of TMA/TMAO ratio in 158KK/308EG individuals showed a considerable reduction in FMO3 activity although they do not show the classical features of trimethylaminuria as a strong body odor and breath.	trimethyloxamine	29-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	102-106
23211429-0	2013	Effects upon in-vivo nicotine metabolism reveal functional variation in FMO3 associated with cigarette consumption.	Nicotine	21-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
23211429-2	2013	Rare mutations in FMO3 are responsible for defective N-oxidation of dietary trimethylamine leading to trimethylaminuria, and common genetic variation in FMO3 has been linked to interindividual variability in metabolic function that may be substrate specific.	Nitrogen	53-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-22
23211429-2	2013	Rare mutations in FMO3 are responsible for defective N-oxidation of dietary trimethylamine leading to trimethylaminuria, and common genetic variation in FMO3 has been linked to interindividual variability in metabolic function that may be substrate specific.	trimethylamine	76-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-22
23211429-3	2013	METHODS: A genetic model of CYP2A6 function is used as a covariate to reveal functional polymorphism in FMO3 that indirectly influences the ratio of deuterated nicotine metabolized to cotinine following oral administration.	Nicotine	160-168	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
23211429-3	2013	METHODS: A genetic model of CYP2A6 function is used as a covariate to reveal functional polymorphism in FMO3 that indirectly influences the ratio of deuterated nicotine metabolized to cotinine following oral administration.	Cotinine	184-192	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
23211429-4	2013	The association is tested between FMO3 haplotype and cigarette consumption in a set of nicotine-dependent smokers.	Nicotine	87-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
23211429-5	2013	RESULTS: FMO3 haplotype, based on all common coding variants in Europeans, significantly predicts nicotine metabolism and accounts for ~2% of variance in the apparent percent of nicotine metabolized to cotinine.	Nicotine	98-106	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
23211429-5	2013	RESULTS: FMO3 haplotype, based on all common coding variants in Europeans, significantly predicts nicotine metabolism and accounts for ~2% of variance in the apparent percent of nicotine metabolized to cotinine.	Nicotine	178-186	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
23211429-5	2013	RESULTS: FMO3 haplotype, based on all common coding variants in Europeans, significantly predicts nicotine metabolism and accounts for ~2% of variance in the apparent percent of nicotine metabolized to cotinine.	Cotinine	202-210	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
23211429-7	2013	Cross-validation demonstrates calculated FMO3 haplotype parameters to be robust and significantly improve the predictive nicotine metabolism model over CYP2A6 genotype alone.	Nicotine	121-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
23211429-8	2013	Functional classes of FMO3 haplotypes, as determined by their influence on nicotine metabolism to cotinine, are also significantly associated with cigarettes per day in nicotine-dependent European Americans (n=1025, P=0.04), and significantly interact (P=0.016) with CYP2A6 genotype to predict cigarettes per day.	Nicotine	75-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-26
23211429-8	2013	Functional classes of FMO3 haplotypes, as determined by their influence on nicotine metabolism to cotinine, are also significantly associated with cigarettes per day in nicotine-dependent European Americans (n=1025, P=0.04), and significantly interact (P=0.016) with CYP2A6 genotype to predict cigarettes per day.	Cotinine	98-106	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-26
23211429-8	2013	Functional classes of FMO3 haplotypes, as determined by their influence on nicotine metabolism to cotinine, are also significantly associated with cigarettes per day in nicotine-dependent European Americans (n=1025, P=0.04), and significantly interact (P=0.016) with CYP2A6 genotype to predict cigarettes per day.	Nicotine	169-177	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-26
23211429-9	2013	CONCLUSION: These findings suggest that common polymorphisms in FMO3 influence nicotine clearance and that these genetic variants in turn influence cigarette consumption.	Nicotine	79-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-68
23430514-1	2013	INTRODUCTION: Trimethylaminuria is a malodour syndrome caused by a functional defect of flavin-containing monoxygenase 3 (FMO3), resulting in accumulation of trimethylamine in body secretions.	trimethylamine	158-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	88-120
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	VX680	125-135	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	226-259
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	VX680	125-135	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	261-266
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	VX680	137-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	226-259
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	VX680	137-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	261-266
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	danusertib	149-159	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	226-259
23358255-1	2013	Aurora kinases were recently identified as a potential target in anticancer therapy and, amongst their available inhibitors, Tozasertib (VX-680) and Danusertib  (PHA-739358) have been indicated as possible substrates of human flavin-containing monooxygenase 3 (hFMO3).	danusertib	149-159	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	261-266
23358255-3	2013	The conversion of Tozasertib and Danusertib to their corresponding metabolites, identified by LC-MS, by the purified  wild-type and V257M hFMO3 show significant differences.	VX680	18-28	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-143
23358255-3	2013	The conversion of Tozasertib and Danusertib to their corresponding metabolites, identified by LC-MS, by the purified  wild-type and V257M hFMO3 show significant differences.	danusertib	33-43	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-143
23430514-1	2013	INTRODUCTION: Trimethylaminuria is a malodour syndrome caused by a functional defect of flavin-containing monoxygenase 3 (FMO3), resulting in accumulation of trimethylamine in body secretions.	trimethylamine	158-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	122-126
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	didodecyldimethylammonium	164-197	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	65-98
23821941-9	2013	Apart from them, UDP-glucuronosyltransferases, cytosolic aldehyde oxidase, amine N-methyltransferase, and flavin-containing monooxygenase 3 are involved in the decomposition of nicotine.	Nicotine	177-185	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-139
23036595-7	2012	CONCLUSIONS: The immobilization of hFMO3 protein in DDAB stabilized AuNP electrodes improves the bioelectrochemical performance of this important phase I drug metabolizing enzyme.	didodecyldimethylammonium	52-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	35-40
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	didodecyldimethylammonium	164-197	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	didodecyldimethylammonium	199-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	65-98
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	didodecyldimethylammonium	199-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	Carbon	215-221	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	65-98
23036595-3	2012	METHODS: In this work, we describe the characterization of human flavin-containing monooxygenase 3 (hFMO3) in a nanoelectrode system based on AuNPs stabilized with didodecyldimethylammonium bromide (DDAB) on glassy carbon electrodes.	Carbon	215-221	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	100-105
23036595-4	2012	Once confirmed by FTIR spectroscopy that in the presence of DDAB-AuNPs the structural integrity of hFMO3 is preserved, the influence of AuNPs on the electrochemistry of the enzyme was studied by cyclic voltammetry and square wave voltammetry.	didodecyldimethylammonium	60-64	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-104
23036595-5	2012	RESULTS: Our results show that AuNPs improve the electrochemical performance of hFMO3 on glassy carbon electrodes by enhancing the electron transfer rate and the current signal-to-noise ratio.	Carbon	96-102	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-85
23036595-6	2012	Moreover, the electrocatalytic activity of hFMO3-DDAB-AuNP electrodes which was investigated in the presence of two well known substrates, benzydamine and sulindac sulfide, resulted in K(M) values of 52muM and 27muM, with V(max) of 8nmolmin(-1)mg(-1) and 4nmolmin(-1)mg(-1), respectively, which are in agreement with data obtained with the microsomal enzyme.	Benzydamine	139-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-48
23036595-6	2012	Moreover, the electrocatalytic activity of hFMO3-DDAB-AuNP electrodes which was investigated in the presence of two well known substrates, benzydamine and sulindac sulfide, resulted in K(M) values of 52muM and 27muM, with V(max) of 8nmolmin(-1)mg(-1) and 4nmolmin(-1)mg(-1), respectively, which are in agreement with data obtained with the microsomal enzyme.	sulindac sulfide	155-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-48
23036595-6	2012	Moreover, the electrocatalytic activity of hFMO3-DDAB-AuNP electrodes which was investigated in the presence of two well known substrates, benzydamine and sulindac sulfide, resulted in K(M) values of 52muM and 27muM, with V(max) of 8nmolmin(-1)mg(-1) and 4nmolmin(-1)mg(-1), respectively, which are in agreement with data obtained with the microsomal enzyme.	8nmolmin	232-240	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-48
23036595-6	2012	Moreover, the electrocatalytic activity of hFMO3-DDAB-AuNP electrodes which was investigated in the presence of two well known substrates, benzydamine and sulindac sulfide, resulted in K(M) values of 52muM and 27muM, with V(max) of 8nmolmin(-1)mg(-1) and 4nmolmin(-1)mg(-1), respectively, which are in agreement with data obtained with the microsomal enzyme.	4nmolmin	255-263	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-48
22576266-2	2012	Moclobemide-N-oxide (65 mg) was the first high-priced metabolite prepared with recombinant hFMO3 on the multi-milligram scale.	Moclobemide-N-Oxide	0-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	91-96
21859392-0	2011	Flavin monooxygenases, FMO1 and FMO3, not cytochrome P450 isoenzymes, contribute to metabolism of anti-tumour triazoloacridinone, C-1305, in liver microsomes and HepG2 cells.	triazoloacridinone	110-128	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	32-36
22387617-8	2012	Significant levels of the novel N-oxide metabolites produced by FMO1 and FMO3 in humans might be associated with the development of procainamide-induced systemic lupus erythematosus.	n-oxide	32-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
22387617-8	2012	Significant levels of the novel N-oxide metabolites produced by FMO1 and FMO3 in humans might be associated with the development of procainamide-induced systemic lupus erythematosus.	Procainamide	132-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
23430919-7	2012	Marked excretions of DMG when the odour had subsided also demonstrate that DMG was not the source of the odour.This patient study raises the possibility that betaine may be converted to TMA by intestinal flora to some degree, resulting in a significant fish odour when oxidation of TMA is compromised by FMO3 variants.	Betaine	158-165	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	304-308
23430919-8	2012	The possibility exists that the body odour occasionally associated with betaine therapy for homocystinuria may not be related to increased circulating betaine or DMG, but due to a common FMO3 mutation resulting in TMAU.	Betaine	72-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	187-191
23430919-8	2012	The possibility exists that the body odour occasionally associated with betaine therapy for homocystinuria may not be related to increased circulating betaine or DMG, but due to a common FMO3 mutation resulting in TMAU.	Trimethylaminuria	214-218	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	187-191
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	NADP	115-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	NADP	115-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	Sulfur	227-233	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	Sulfur	227-233	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	Nitrogen	237-245	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-39
22177984-1	2012	Human flavin-containing monooxygenase 3 (hFMO3) is a microsomal drug-metabolizing monooxygenase that catalyzes the NADPH-dependent oxygenation of a wide range of drugs and xenobiotics which contain a soft-nucleophiles, usually sulfur or nitrogen.	Nitrogen	237-245	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-46
22177984-4	2012	The tr-hFMO3 proves to be detached from the membrane, properly folded and fully active towards well-known marker substrates such as benzydamine and sulindac sulfide with measured apparent K(m) values of 45 +- 8 muM and 25 +- 4 muM, respectively.	Benzydamine	132-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-12
22177984-4	2012	The tr-hFMO3 proves to be detached from the membrane, properly folded and fully active towards well-known marker substrates such as benzydamine and sulindac sulfide with measured apparent K(m) values of 45 +- 8 muM and 25 +- 4 muM, respectively.	sulindac sulfide	148-164	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-12
21859392-3	2011	We demonstrated that the studied triazoloacridinone was transformed with rat and human liver microsomes, HepG2 hepatoma cells and with human recombinant flavin-containing monooxygenases FMO1, FMO3 but not with CYPs.	triazoloacridinone	33-51	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	192-196
21859392-8	2011	In contrast, FMO1 and FMO3 were crucial for metabolism of C-1305 by liver microsomes and in HepG2 cells, which makes C-1305 an attractive potent anti-tumour agent.	C 1305	58-64	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-26
21395651-5	2011	RESULTS: There was a significant correlation between trimethylamine N-oxygenation functional activity and FMO3 expression levels in human liver microsomes (r= 0.71, P < 0.05, n= 9).	trimethylamine	53-67	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
20182906-10	2011	However, the relationship between FMO3 polymorphisms and clearance of danusertib warrants further research, as we could study only a small group of patients.	danusertib	70-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
21395651-6	2011	Trimethylamine N-oxygenation was catalyzed largely by FMO3 and not by FMO1 or FMO5.	trimethylamine n	0-16	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
20570689-8	2010	The protein synthesis inhibitor, cycloheximide (which causes "superinduction" of CYP1A1 mRNA in TCDD-treated cells), by itself caused dramatic upregulation (>300-fold) of FMO3 mRNA in Hepa-1 suggesting that cycloheximide prevents synthesis of a labile protein that suppresses FMO3 expression.	Cycloheximide	33-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-178
21226652-12	2011	Multiple enzymes including CYP2D6, CYP3A4/5, FMO1 and FMO3 catalyzed AZD0328 metabolism.	spiro(1-azabicyclo(2.2.2)octane-3,2'(3H)-furo(2,3-b)pyridine)	69-76	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
20947616-10	2011	This metabolic reaction was also inhibited by BNPP or a brief heat treatment at 50 C. Methimazole, the substrate/inhibitor of FMO1 and FMO3, did not inhibit this reaction.	Methimazole	86-97	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	135-139
20810540-7	2010	Of interest, the FMO3 enzymes showed a 2-fold activation of k(cat)/K(m) in the presence of Triton X-100.	Octoxynol	91-103	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	17-21
20810540-8	2010	Oligomeric analysis of MBP-FMO3 also showed disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100.	Octoxynol	134-146	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
20652542-2	2010	Here we report a simple but functional and stable enzyme-electrode system based on a glassy carbon (GC) electrode with human flavin-containing monooxygenase isoform 3 (hFMO3) entrapped in a gel cross-linked with bovine serum albumin (BSA) by glutaraldehyde.	Carbon	92-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	168-173
20652542-2	2010	Here we report a simple but functional and stable enzyme-electrode system based on a glassy carbon (GC) electrode with human flavin-containing monooxygenase isoform 3 (hFMO3) entrapped in a gel cross-linked with bovine serum albumin (BSA) by glutaraldehyde.	Glutaral	242-256	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	168-173
20570689-8	2010	The protein synthesis inhibitor, cycloheximide (which causes "superinduction" of CYP1A1 mRNA in TCDD-treated cells), by itself caused dramatic upregulation (>300-fold) of FMO3 mRNA in Hepa-1 suggesting that cycloheximide prevents synthesis of a labile protein that suppresses FMO3 expression.	Cycloheximide	33-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	279-283
20570689-8	2010	The protein synthesis inhibitor, cycloheximide (which causes "superinduction" of CYP1A1 mRNA in TCDD-treated cells), by itself caused dramatic upregulation (>300-fold) of FMO3 mRNA in Hepa-1 suggesting that cycloheximide prevents synthesis of a labile protein that suppresses FMO3 expression.	Polychlorinated Dibenzodioxins	96-100	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-178
20570689-8	2010	The protein synthesis inhibitor, cycloheximide (which causes "superinduction" of CYP1A1 mRNA in TCDD-treated cells), by itself caused dramatic upregulation (>300-fold) of FMO3 mRNA in Hepa-1 suggesting that cycloheximide prevents synthesis of a labile protein that suppresses FMO3 expression.	Cycloheximide	210-223	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-178
19571433-2	2009	Significant correlations were observed for benzydamine N-oxygenation or methyl p-tolyl sulfide S-oxygenation activity (in the range of approximately 20- to approximately 40-fold) and FMO3 levels determined immunochemically in liver microsomes (r(2)=0.73-0.75, p<0.0001, n=16).	benzydamine n	43-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	183-187
19841059-3	2010	Voriconazole is cleared predominantly via hepatic metabolism in adults, mainly by CYP3A4, CYP2C19, and flavin-containing monooxygenase 3 (FMO3).	Voriconazole	0-12	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	103-136
19841059-3	2010	Voriconazole is cleared predominantly via hepatic metabolism in adults, mainly by CYP3A4, CYP2C19, and flavin-containing monooxygenase 3 (FMO3).	Voriconazole	0-12	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
19841059-9	2010	Although expression of CYP2C19 and FMO3 is not significantly different in children versus adults, these enzymes seem to contribute to higher metabolic clearance of voriconazole in children versus adults.	Voriconazole	164-176	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	35-39
19552509-5	2009	The Michaelis-Menten kinetic constants for DMA N-oxidation by FMO1 were: K(m) of 44.5 microM, V(max) of 7.59 nmol min(-1) mg(-1) protein, and intrinsic clearance of 171 microl min(-1) mg(-1) protein, which was about twelve-fold higher than that by FMO3.	dimethylamphetamine	43-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	248-252
20198379-0	2010	A common FMO3 polymorphism may amplify the effect of nicotine exposure in sudden infant death syndrome (SIDS).	Nicotine	53-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
20198379-4	2010	The flavin-monooxygenase 3 (FMO3) is one of the enzymes metabolising nicotine, and several polymorphisms have already been described in this gene.	Nicotine	69-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-26
20198379-4	2010	The flavin-monooxygenase 3 (FMO3) is one of the enzymes metabolising nicotine, and several polymorphisms have already been described in this gene.	Nicotine	69-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	28-32
20028087-2	2010	Glassy carbon and gold electrodes gave reversible electrochemical signals of an active hFMO3.	Carbon	7-13	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-92
20028087-4	2010	A monolayer coverage was obtained on gold functionalized with dithio-bismaleimidoethane that covalently linked surface accessible cysteines of hFMO3.	dithiobis(N-ethylmaleimide)	62-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	143-148
20028087-4	2010	A monolayer coverage was obtained on gold functionalized with dithio-bismaleimidoethane that covalently linked surface accessible cysteines of hFMO3.	Cysteine	130-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	143-148
20028087-8	2010	In the case of benzydamine, a K(M) of 44 +/- 5 microM was measured upon application of a -600 mV bias to the enzyme immobilized on the glassy carbon electrode that is in good agreement with the values published for microsomal hFMO3 where NADPH is the electron donor.	Benzydamine	15-26	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	226-231
20028087-8	2010	In the case of benzydamine, a K(M) of 44 +/- 5 microM was measured upon application of a -600 mV bias to the enzyme immobilized on the glassy carbon electrode that is in good agreement with the values published for microsomal hFMO3 where NADPH is the electron donor.	Carbon	142-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	226-231
19881207-3	2009	Malodorous trimethylamine is generally converted to odorless trimethylamine N-oxide by liver microsomal FMO3.	malodorous trimethylamine	0-25	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
19881207-3	2009	Malodorous trimethylamine is generally converted to odorless trimethylamine N-oxide by liver microsomal FMO3.	trimethyloxamine	61-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	104-108
19881207-11	2009	These lines of evidence suggest that individual differences of FMO3 are important determinants for the metabolic fate of dietary-derived trimethylamine.	trimethylamine	137-151	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
19635782-7	2009	Benzydamine N-oxidation catalyzed by hFMO3 showed values of 42.6 microM (K(m)) and 3.56 nmol/min/nmol of enzyme (V(max)).	benzydamine n	0-13	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-42
19635782-8	2009	Human FMO3 was observed to catalyze the S-oxidation of sulindac sulfide, with respective K(m) and V(max) values of 69.3 microM and 35.4 nmol/min/nmol of enzyme.	sulindac sulfide	55-71	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
19635782-11	2009	In summary, dFMO3 appears to be a functional enzyme expressed at appreciable levels in liver, but one with some kinetic properties that are substantially different from its human homolog hFMO3.	dfmo3	12-17	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	187-192
19577495-8	2009	Analysis of the mutant FMO3 expressed in bacteria revealed that the R238Q mutation abolished catalytic activity of the enzyme and is thus a causative mutation for TMAuria.	Trimethylaminuria	163-170	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	23-27
19577495-9	2009	The specificity constant (k(cat)/K(M)) of the K158/G308 variant was 43% of that of ancestral FMO3.	2-Amino-5-bromo-3-nitropyridine	46-50	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	93-97
19577495-9	2009	The specificity constant (k(cat)/K(M)) of the K158/G308 variant was 43% of that of ancestral FMO3.	g308	51-55	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	93-97
19321370-3	2009	In a healthy individual, 95% or more of TMA is converted by the flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) to non-odorous trimethylamine N-oxide (TMA N-oxide).	trimethylamine	40-43	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-97
19321370-3	2009	In a healthy individual, 95% or more of TMA is converted by the flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) to non-odorous trimethylamine N-oxide (TMA N-oxide).	trimethylamine	40-43	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
19321370-3	2009	In a healthy individual, 95% or more of TMA is converted by the flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) to non-odorous trimethylamine N-oxide (TMA N-oxide).	trimethyloxamine	134-156	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
19321370-3	2009	In a healthy individual, 95% or more of TMA is converted by the flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) to non-odorous trimethylamine N-oxide (TMA N-oxide).	trimethyloxamine	158-169	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	64-97
19321370-3	2009	In a healthy individual, 95% or more of TMA is converted by the flavin-containing monooxygenase 3 (FMO3, EC 1.14.13.8) to non-odorous trimethylamine N-oxide (TMA N-oxide).	trimethyloxamine	158-169	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
19321370-4	2009	Several single nucleotide polymorphisms (SNPs) of the FMO3 gene have been described and result in an enzyme with decreased or abolished functional activity for TMA N-oxygenation thus leading to TMAu.	trimethylamine	160-163	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
19321370-4	2009	Several single nucleotide polymorphisms (SNPs) of the FMO3 gene have been described and result in an enzyme with decreased or abolished functional activity for TMA N-oxygenation thus leading to TMAu.	Trimethylaminuria	194-198	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
19321370-6	2009	Sequence analysis of the exon regions of the FMO3 gene of a young woman with severe TMAu revealed heterozygous mutations at positions 187 (V187A), 158 (E158K), 308 (E308G), and 305 (E305X).	Trimethylaminuria	84-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	45-49
19321370-8	2009	FMO3 variants V187A and V187A/E158K were characterized for oxygenation of several common FMO3 substrates (i.e., 5- and 8-DPT, mercaptoimidazole (MMI), TMA, and sulindac sulfide) and for its thermal stability.	5- and 8-dpt	112-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
19321370-8	2009	FMO3 variants V187A and V187A/E158K were characterized for oxygenation of several common FMO3 substrates (i.e., 5- and 8-DPT, mercaptoimidazole (MMI), TMA, and sulindac sulfide) and for its thermal stability.	1-benzyl-4-isocyanatobenzene	145-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
19321370-8	2009	FMO3 variants V187A and V187A/E158K were characterized for oxygenation of several common FMO3 substrates (i.e., 5- and 8-DPT, mercaptoimidazole (MMI), TMA, and sulindac sulfide) and for its thermal stability.	trimethylamine	151-154	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
19321370-8	2009	FMO3 variants V187A and V187A/E158K were characterized for oxygenation of several common FMO3 substrates (i.e., 5- and 8-DPT, mercaptoimidazole (MMI), TMA, and sulindac sulfide) and for its thermal stability.	sulindac sulfide	160-176	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
19321370-9	2009	Our findings show that with the combination of V187A/E158K mutations in FMO3, the enzyme activity is severely affected and possibly contributes to the TMAu observed.	Trimethylaminuria	151-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
19283698-7	2009	FMO1 produces more (-)-CSO-enantiomer, while FMO3 generates mainly (+)-CSO-enantiomer.	(+)-cso-enantiomer	67-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	45-49
18948378-3	2009	The metabolites generated, the sulfenic acid, sulfinic acid, and carbodiimide derivatives, are the same as those produced by EtaA and human FMO1 and FMO3.	Sulfenic Acids	31-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	149-153
18948378-3	2009	The metabolites generated, the sulfenic acid, sulfinic acid, and carbodiimide derivatives, are the same as those produced by EtaA and human FMO1 and FMO3.	Sulfinic Acids	46-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	149-153
18948378-3	2009	The metabolites generated, the sulfenic acid, sulfinic acid, and carbodiimide derivatives, are the same as those produced by EtaA and human FMO1 and FMO3.	Carbodiimides	65-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	149-153
19571433-3	2009	Preincubation with the reducing agent ascorbate revealed that FMO3 activity in some liver samples is suppressed.	Ascorbic Acid	38-47	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-66
18942155-7	2008	The developed electrophoretically mediated microanalysis method was applied for the kinetics study of FMO3 using clozapine as a substrate probe.	Clozapine	113-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	102-106
18930751-0	2008	Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes.	Ethionamide	41-52	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-91
18775983-6	2008	The resulting protein had similar mobility (approximately 56 kDa) as isolated rat liver FMO3 and cDNA-expressed human FMO3 by SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	126-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	118-122
18775983-6	2008	The resulting protein had similar mobility (approximately 56 kDa) as isolated rat liver FMO3 and cDNA-expressed human FMO3 by SDS-polyacrylamide gel electrophoresis.	polyacrylamide	130-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	118-122
18188833-6	2008	CYP3A4 isozyme showed the broadest metabolic capacity, whereas CYP1A1, CYP1B1 and FMO3 isozymes biotransformed imatinib with a high intrinsic clearance.	Imatinib Mesylate	111-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	82-86
18157663-1	2008	A bioelectronic sensor for triethylamine (TEA) was developed with a flavin-containing monooxygenase type 3 (FMO-3).	triethylamine	27-40	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-113
18157663-1	2008	A bioelectronic sensor for triethylamine (TEA) was developed with a flavin-containing monooxygenase type 3 (FMO-3).	triethylamine	42-45	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-113
18157663-2	2008	The TEA biosensor consisted of a Clark-type dissolved-oxygen electrode and an FMO-3 immobilized membrane.	triethylamine	4-7	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	78-83
18157663-7	2008	A drop of the phosphate buffer solution with the AsA was put on the sensing area of the oxygen electrode, and the FMO-3 immobilized membrane was placed on the oxygen electrode and covered with a supporting Nylon mesh net which was secured with a silicone O-ring.	Oxygen	159-165	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	114-119
18157663-7	2008	A drop of the phosphate buffer solution with the AsA was put on the sensing area of the oxygen electrode, and the FMO-3 immobilized membrane was placed on the oxygen electrode and covered with a supporting Nylon mesh net which was secured with a silicone O-ring.	Silicones	246-254	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	114-119
18157663-9	2008	The FMO-3 biosensor was used to measure TEA solution from 0.5 to 4.0 mmol L(-1) with 10.0 mmol L(-1) AsA.	triethylamine	40-43	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-9
18157663-9	2008	The FMO-3 biosensor was used to measure TEA solution from 0.5 to 4.0 mmol L(-1) with 10.0 mmol L(-1) AsA.	Ascorbic Acid	101-104	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-9
18362161-9	2008	Kinetic analysis of voriconazole metabolism by FMO1 and FMO3 yielded K(m) values of 3.0 and 3.4 mM and V(max) values of 0.025 and 0.044 pmol/min/pmol, respectively.	Voriconazole	20-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	56-60
19356079-0	2008	Analysis of flavin-containing monooxygenase 3 genotype data in populations administered the anti-schizophrenia agent olanzapine.	Olanzapine	117-127	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-45
19356079-2	2008	Single nucleotide polymorphisms and haplotypes associated with case-control status was undertaken to determine the potential role of FMO3 in olanzapine therapeutic response.	Olanzapine	141-151	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	133-137
17881660-7	2007	FMO3 was the primary enzyme responsible for TG100855 formation.	(7-(2,6-dichlorophenyl)-5-methylbenzo(1,2,4)triazin-3-yl)-(4-(2-(1-oxypyrrolidin-1-yl)ethoxy)phenyl)amine	44-52	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)-L-cysteine sulfoxide	42-84	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-160
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)-L-cysteine sulfoxide	42-84	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)-L-cysteine sulfoxide	86-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-160
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)-L-cysteine sulfoxide	86-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	42-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-160
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	42-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	86-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-160
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	86-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	224-228	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-160
17892265-1	2007	Previously, our laboratory has shown that S-(1,2-dichlorovinyl)-L-cysteine sulfoxide (DCVCS), a Michael acceptor produced by a flavin-containing monooxygenase 3 (FMO3)-mediated oxidation of S-(1,2-dichlorovinyl)-L-cysteine (DCVC), is a more potent nephrotoxicant than DCVC.	S-(1,2-dichlorovinyl)cysteine	224-228	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	162-166
17584019-8	2007	In addition, other causal factors for decreased FMO3 metabolic capacity such as liver damage or menstruation and treatment with copper chlorophyllin are also included in this minireview.	chlorophyllin	128-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
17531949-1	2007	Impaired conversion of trimethylamine to trimethylamine N-oxide by human flavin containing monooxygenase 3 (FMO3) is strongly associated with primary trimethylaminuria, also known as "fish-odor" syndrome.	trimethylamine	23-37	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-106
17531949-1	2007	Impaired conversion of trimethylamine to trimethylamine N-oxide by human flavin containing monooxygenase 3 (FMO3) is strongly associated with primary trimethylaminuria, also known as "fish-odor" syndrome.	trimethylamine	23-37	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	108-112
17531949-1	2007	Impaired conversion of trimethylamine to trimethylamine N-oxide by human flavin containing monooxygenase 3 (FMO3) is strongly associated with primary trimethylaminuria, also known as "fish-odor" syndrome.	trimethyloxamine	41-63	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-106
17531949-1	2007	Impaired conversion of trimethylamine to trimethylamine N-oxide by human flavin containing monooxygenase 3 (FMO3) is strongly associated with primary trimethylaminuria, also known as "fish-odor" syndrome.	trimethyloxamine	41-63	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	108-112
17257434-3	2007	METHODS: FMO3 metabolic capacity (conversion of trimethylamine to trimethylamine N-oxide) was defined as the urinary ratio of trimethylamine N-oxide to total trimethylamine.	trimethylamine	48-62	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
17559352-6	2007	Two commonly occurring polymorphisms of FMO3, E158K and E308G, have been associated with a reduction in polyp burden in patients with familial adenomatous polyposis who were treated with sulindac sulfide, an FMO3 substrate.	sulindac sulfide	187-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
17142560-1	2007	The decreased capacity of the flavin-containing monooxygenase 3 (FMO3) to oxygenate xenobiotics including trimethylamine is believed to contribute to metabolic disorders.	trimethylamine	106-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-63
17142560-1	2007	The decreased capacity of the flavin-containing monooxygenase 3 (FMO3) to oxygenate xenobiotics including trimethylamine is believed to contribute to metabolic disorders.	trimethylamine	106-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	65-69
17142560-3	2007	Recombinant Glu158Lys and Glu158Lys-Glu308Gly FMO3 expressed in Escherichia coli membranes showed slightly decreased N-oxygenation of benzydamine and trimethylamine.	Benzydamine	134-145	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
17142560-3	2007	Recombinant Glu158Lys and Glu158Lys-Glu308Gly FMO3 expressed in Escherichia coli membranes showed slightly decreased N-oxygenation of benzydamine and trimethylamine.	trimethylamine	150-164	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
17142560-6	2007	Val257Met FMO3 had a lower catalytic efficiency for methyl p-tolyl sulfide and sulindac sulfide S-oxygenation.	methyl 4-tolylsulfide	52-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	10-14
17142560-6	2007	Val257Met FMO3 had a lower catalytic efficiency for methyl p-tolyl sulfide and sulindac sulfide S-oxygenation.	sulindac sulfide	79-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	10-14
17142560-7	2007	However, compared with wild-type FMO3, Val257Met FMO3 showed a similar catalytic efficiency for N-oxygenation of benzydamine and trimethylamine.	Benzydamine	113-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	33-37
17142560-7	2007	However, compared with wild-type FMO3, Val257Met FMO3 showed a similar catalytic efficiency for N-oxygenation of benzydamine and trimethylamine.	Benzydamine	113-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-53
17142560-7	2007	However, compared with wild-type FMO3, Val257Met FMO3 showed a similar catalytic efficiency for N-oxygenation of benzydamine and trimethylamine.	trimethylamine	129-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	33-37
17142560-7	2007	However, compared with wild-type FMO3, Val257Met FMO3 showed a similar catalytic efficiency for N-oxygenation of benzydamine and trimethylamine.	trimethylamine	129-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-53
17142560-8	2007	The catalytic efficiency for benzydamine and trimethylamine N-oxygenation by Arg205Cys FMO3 was only moderately decreased, but it possessed decreased sulindac sulfide S-oxygenation activity.	Benzydamine	29-40	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-91
17142560-8	2007	The catalytic efficiency for benzydamine and trimethylamine N-oxygenation by Arg205Cys FMO3 was only moderately decreased, but it possessed decreased sulindac sulfide S-oxygenation activity.	trimethylamine	45-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-91
17142560-8	2007	The catalytic efficiency for benzydamine and trimethylamine N-oxygenation by Arg205Cys FMO3 was only moderately decreased, but it possessed decreased sulindac sulfide S-oxygenation activity.	sulindac sulfide	150-166	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-91
17142560-9	2007	Kinetic analysis showed that Arg205Cys FMO3 was inhibited by sulindac in a substrate-dependent manner, presumably because of selective interaction between the variant enzyme and the substrate.	Sulindac	61-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	39-43
17257434-3	2007	METHODS: FMO3 metabolic capacity (conversion of trimethylamine to trimethylamine N-oxide) was defined as the urinary ratio of trimethylamine N-oxide to total trimethylamine.	trimethyloxamine	66-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
17257434-3	2007	METHODS: FMO3 metabolic capacity (conversion of trimethylamine to trimethylamine N-oxide) was defined as the urinary ratio of trimethylamine N-oxide to total trimethylamine.	trimethyloxamine	126-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
17257434-3	2007	METHODS: FMO3 metabolic capacity (conversion of trimethylamine to trimethylamine N-oxide) was defined as the urinary ratio of trimethylamine N-oxide to total trimethylamine.	trimethylamine	66-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
16963488-2	2006	FMO3, the primary isoform expressed in adult human liver, has the lowest Km and favors methionine-d-sulfoxide (Met-d-O) formation over methionine-l-sulfoxide.	methionine-d-sulfoxide	87-109	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
17050781-4	2007	Using expressed recombinant enzyme with methimazole, trimethylamine, sulindac, and ethylenethiourea, the novel structural variants FMO3 E24D and K416N were shown to cause modest changes in catalytic efficiency, whereas a third novel variant, FMO3 N61K, was essentially devoid of activity.	Methimazole	40-51	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
17050781-4	2007	Using expressed recombinant enzyme with methimazole, trimethylamine, sulindac, and ethylenethiourea, the novel structural variants FMO3 E24D and K416N were shown to cause modest changes in catalytic efficiency, whereas a third novel variant, FMO3 N61K, was essentially devoid of activity.	trimethylamine	53-67	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
17050781-4	2007	Using expressed recombinant enzyme with methimazole, trimethylamine, sulindac, and ethylenethiourea, the novel structural variants FMO3 E24D and K416N were shown to cause modest changes in catalytic efficiency, whereas a third novel variant, FMO3 N61K, was essentially devoid of activity.	Sulindac	69-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
17050781-4	2007	Using expressed recombinant enzyme with methimazole, trimethylamine, sulindac, and ethylenethiourea, the novel structural variants FMO3 E24D and K416N were shown to cause modest changes in catalytic efficiency, whereas a third novel variant, FMO3 N61K, was essentially devoid of activity.	Ethylenethiourea	83-99	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
17050781-4	2007	Using expressed recombinant enzyme with methimazole, trimethylamine, sulindac, and ethylenethiourea, the novel structural variants FMO3 E24D and K416N were shown to cause modest changes in catalytic efficiency, whereas a third novel variant, FMO3 N61K, was essentially devoid of activity.	Ethylenethiourea	83-99	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	242-246
16985102-6	2006	Compared with wild-type FMO3, the Ala360-FMO3 and His360-FMO3 variants were less catalytically efficient for mercaptoimidazole S-oxygenation.	2-mercaptoimidazole	109-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	24-28
16985102-6	2006	Compared with wild-type FMO3, the Ala360-FMO3 and His360-FMO3 variants were less catalytically efficient for mercaptoimidazole S-oxygenation.	2-mercaptoimidazole	109-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
16985102-6	2006	Compared with wild-type FMO3, the Ala360-FMO3 and His360-FMO3 variants were less catalytically efficient for mercaptoimidazole S-oxygenation.	2-mercaptoimidazole	109-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
16985102-7	2006	N-Oxygenation of chlorpromazine was significantly less catalytically efficient for His360-FMO3 compared with wild-type FMO3.	Chlorpromazine	17-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-94
16985102-7	2006	N-Oxygenation of chlorpromazine was significantly less catalytically efficient for His360-FMO3 compared with wild-type FMO3.	Chlorpromazine	17-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	119-123
16985102-12	2006	The increase in catalytic efficiency observed for Pro360 in human FMO3 was also observed when the His of FMO1 was replaced by Pro at loci 360.	Histidine	98-101	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
16963488-2	2006	FMO3, the primary isoform expressed in adult human liver, has the lowest Km and favors methionine-d-sulfoxide (Met-d-O) formation over methionine-l-sulfoxide.	met-d-o	111-118	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
16963488-2	2006	FMO3, the primary isoform expressed in adult human liver, has the lowest Km and favors methionine-d-sulfoxide (Met-d-O) formation over methionine-l-sulfoxide.	methionine-l-sulfoxide	135-157	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
16857727-5	2006	In addition, recombinant FMO1 and FMO3 were able to bioactivate both SMX and DDS, resulting in covalent adduct formation.	Sulfamethoxazole	69-72	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
16985102-12	2006	The increase in catalytic efficiency observed for Pro360 in human FMO3 was also observed when the His of FMO1 was replaced by Pro at loci 360.	Proline	50-53	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
17159773-0	2006	Experimental approaches to studies on drug metabolism and drug interactions in man: interaction of acyclic nucleoside phosphonates with human liver cytochromes P450 and flavin-containing monooxygenase 3.	nucleoside phosphonates	107-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	148-202
17159773-1	2006	OBJECTIVES: To determine a possible influence of acyclic nucleoside phosphonates on FMO3 and CYP activity at molecular level in vitro.	acyclic	49-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	84-88
17159773-1	2006	OBJECTIVES: To determine a possible influence of acyclic nucleoside phosphonates on FMO3 and CYP activity at molecular level in vitro.	nucleoside phosphonates	57-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	84-88
17159773-3	2006	RESULTS: Activity of FMO3 was inhibited by PMPA and bisPOC-PMPA even at low levels of these drugs (below 100 microM).	Tenofovir	43-47	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	21-25
17159773-3	2006	RESULTS: Activity of FMO3 was inhibited by PMPA and bisPOC-PMPA even at low levels of these drugs (below 100 microM).	bis(isopropyloxymethylcarbonyl) 9-(2-phosphonomethoxypropyl)adenine	52-63	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	21-25
17159773-6	2006	CONCLUSIONS: PMPA and bisPOC-PMPA are able to inhibit FMO3 activity at relatively low levels (10-100 microM) indicating a relatively specific interaction.	Tenofovir	13-17	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
17159773-6	2006	CONCLUSIONS: PMPA and bisPOC-PMPA are able to inhibit FMO3 activity at relatively low levels (10-100 microM) indicating a relatively specific interaction.	bis(isopropyloxymethylcarbonyl) 9-(2-phosphonomethoxypropyl)adenine	22-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
17159773-9	2006	As the inhibitor concentration in the systemic circulation does not exceed 2 microM, the probability of a significant in vivo effect of adefovir, tenofovir and the respective prodrugs on the microsomal system of cytochromes P450 and FMO3 is relatively low.	adefovir	136-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	233-237
17159773-9	2006	As the inhibitor concentration in the systemic circulation does not exceed 2 microM, the probability of a significant in vivo effect of adefovir, tenofovir and the respective prodrugs on the microsomal system of cytochromes P450 and FMO3 is relatively low.	Tenofovir	146-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	233-237
16857727-5	2006	In addition, recombinant FMO1 and FMO3 were able to bioactivate both SMX and DDS, resulting in covalent adduct formation.	Fumigant 93	77-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
16857727-10	2006	Thus, our results suggest an important role for FMO3 and yet-to-be identified peroxidases in the bioactivation of sulfonamides in NHEKs.	Sulfonamides	114-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
16864509-0	2006	Bioactivation of N-substituted N"-(4-imidazole-ethyl)thioureas by human FMO1 and FMO3.	n-substituted n"-(4-imidazole-ethyl)thioureas	17-62	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	81-85
16864509-2	2006	A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3.	Thiourea	145-153	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	193-197
16864509-1	2006	Enzyme kinetic parameters of the bioactivation of thiourea-containing compounds by human flavin-containing monooxygenase enzymes (FMOs) FMO1 and FMO3 were investigated.	Thiourea	50-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	145-149
16864509-3	2006	The results show that major differences in enzyme kinetic parameters for N-substituted N"-(4-imidazole-ethyl)thiourea exist between human FMO3 and human FMO1.	n-substituted n"-(4-imidazole-ethyl)thiourea	73-117	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
16864509-4	2006	Whereas Km values of N-substituted N"-(4-imidazole-ethyl)thioureas for human FMO3 are all in the millimolar range, the Km values for human FMO1 range from the low micromolar to the low millimolar range.	n-substituted n"-(4-imidazole-ethyl)thioureas	21-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-81
16864509-2	2006	A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3.	Thiourea	63-71	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	193-197
16864509-5	2006	Furthermore, among a series of N-p-phenyl-substituted N"-(4-imidazole-ethyl)thioureas an interesting structure-activity relationship is evident with both FMO1 and FMO3.	n-p-phenyl-substituted n"-(4-imidazole-ethyl)thioureas	31-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	163-167
16864509-2	2006	A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3.	Thiocholine	95-106	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	193-197
16864509-8	2006	Enzyme kinetic parameters Km and kcat/Km of human FMO1 for N-substituted N"-(4-imidazole-ethyl)thioureas show a high degree of correlation with the results obtained in rat liver microsomes, in which rat FMO1 is the most abundant form, whereas those of human FMO3 do not.	n-substituted n"-(4-imidazole-ethyl)thioureas	59-104	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	258-262
16858129-3	2006	The Thr(201)Lys and Met(260)Val also presented together with known SNPs (Glu(158)Lys-Glu(308)Gly and Val(257)Met, respectively) in the same alleles of the FMO3 gene to form novel haplotypes.	Glutamic Acid	73-76	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	155-159
16858129-3	2006	The Thr(201)Lys and Met(260)Val also presented together with known SNPs (Glu(158)Lys-Glu(308)Gly and Val(257)Met, respectively) in the same alleles of the FMO3 gene to form novel haplotypes.	Lysine	12-15	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	155-159
16858129-3	2006	The Thr(201)Lys and Met(260)Val also presented together with known SNPs (Glu(158)Lys-Glu(308)Gly and Val(257)Met, respectively) in the same alleles of the FMO3 gene to form novel haplotypes.	Glutamic Acid	85-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	155-159
16858129-3	2006	The Thr(201)Lys and Met(260)Val also presented together with known SNPs (Glu(158)Lys-Glu(308)Gly and Val(257)Met, respectively) in the same alleles of the FMO3 gene to form novel haplotypes.	Glycine	93-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	155-159
16858129-4	2006	A SNP (30,398 C>T) in the FMO3 gene causing a stop codon at Arg(500) in exon 9 was also discovered.	Arginine	63-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-33
16481213-3	2006	Mutations in the FMO3 gene can result in defective trimethylamine (TMA) N-oxygenation, which gives rise to the disorder known as trimethylaminuria (TMAU) or "fish-odour syndrome".	trimethylamine	51-65	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	17-21
15547051-11	2005	The relative contribution of FMO1 and FMO3 to the sulfoxidation of carbophenothion, demeton-O, ethiofencarb, fonofos, and methiocarb also was investigated by using baculovirus-expressed recombinant proteins.	carbophenothion	67-82	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	38-42
16544950-0	2006	Oxidative activation of thiacetazone by the Mycobacterium tuberculosis flavin monooxygenase EtaA and human FMO1 and FMO3.	Thioacetazone	24-36	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
16214918-0	2005	Genetic polymorphisms of flavin monooxygenase 3 in sulindac-induced regression of colorectal adenomas in familial adenomatous polyposis.	Sulindac	51-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	25-47
16214918-2	2005	In vivo, the active form of sulindac is sulindac sulfide, which is inactivated by the hepatic microsomal enzyme, flavin monooxygenase 3 (FMO3).	Sulindac	28-36	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-135
16214918-2	2005	In vivo, the active form of sulindac is sulindac sulfide, which is inactivated by the hepatic microsomal enzyme, flavin monooxygenase 3 (FMO3).	Sulindac	28-36	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
16214918-2	2005	In vivo, the active form of sulindac is sulindac sulfide, which is inactivated by the hepatic microsomal enzyme, flavin monooxygenase 3 (FMO3).	sulindac sulfide	40-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-135
16214918-2	2005	In vivo, the active form of sulindac is sulindac sulfide, which is inactivated by the hepatic microsomal enzyme, flavin monooxygenase 3 (FMO3).	sulindac sulfide	40-56	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
16214918-4	2005	We recently showed that certain polymorphic forms of FMO3 with reduced activity were associated with a more favorable response to sulindac in preventing the formation of adenomas in patients with FAP without polyps at baseline.	Sulindac	130-138	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	53-57
16214918-5	2005	Here, we determined whether these FMO3 polymorphisms correlated with the ability of sulindac to regress polyposis in patients with FAP who had polyps prior to treatment.	Sulindac	84-92	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	34-38
15987777-0	2005	Oxidation of tamoxifen by human flavin-containing monooxygenase (FMO) 1 and FMO3 to tamoxifen-N-oxide and its novel reduction back to tamoxifen by human cytochromes P450 and hemoglobin.	Tamoxifen	13-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
15987777-0	2005	Oxidation of tamoxifen by human flavin-containing monooxygenase (FMO) 1 and FMO3 to tamoxifen-N-oxide and its novel reduction back to tamoxifen by human cytochromes P450 and hemoglobin.	tamoxifen N-oxide	84-101	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
15987777-0	2005	Oxidation of tamoxifen by human flavin-containing monooxygenase (FMO) 1 and FMO3 to tamoxifen-N-oxide and its novel reduction back to tamoxifen by human cytochromes P450 and hemoglobin.	Tamoxifen	84-93	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
15987777-3	2005	The current study demonstrates that human FMO1 and FMO3 catalyze TAM N-oxidation to TNO and that cytochromes P450 (P450s), but not FMOs, reduce TNO to TAM.	Tamoxifen	65-68	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	51-55
15734728-6	2005	Enzymes involved in nicotine metabolism including cytochrome P450 enzymes, aldehyde oxidase, flavin-containing monooxygenase 3, amine N-methyltransferase, and UDP-glucuronosyltransferases are represented, as well as factors affecting metabolism, such as genetic variations in metabolic enzymes, effects of diet, age, gender, pregnancy, liver and kidney diseases, and racial and ethnic differences.	Nicotine	20-28	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	93-126
16601883-1	2006	Persistent trimethylaminuria in children is caused by autosomal recessively inherited impairment of hepatic trimethylamine (TMA) oxidation due to deficiency of flavin monooxygenase 3 (FMO3) secondary to mutations in the FMO3 gene.	trimethylamine	108-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	160-182
16601883-1	2006	Persistent trimethylaminuria in children is caused by autosomal recessively inherited impairment of hepatic trimethylamine (TMA) oxidation due to deficiency of flavin monooxygenase 3 (FMO3) secondary to mutations in the FMO3 gene.	trimethylamine	108-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	184-188
16601883-1	2006	Persistent trimethylaminuria in children is caused by autosomal recessively inherited impairment of hepatic trimethylamine (TMA) oxidation due to deficiency of flavin monooxygenase 3 (FMO3) secondary to mutations in the FMO3 gene.	trimethylamine	108-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	220-224
16601883-10	2006	A further patient, heterozygous for two novel sequence variations in the FMO3 gene, consistently showed malodour and elevated urinary TMA/TMAO ratios under basal conditions but a negative response to both choline and marine fish meal loading.	trimethyloxamine	138-142	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
16601883-10	2006	A further patient, heterozygous for two novel sequence variations in the FMO3 gene, consistently showed malodour and elevated urinary TMA/TMAO ratios under basal conditions but a negative response to both choline and marine fish meal loading.	Choline	205-212	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
16684653-8	2006	We collaborated with Dr. Kupfer"s laboratory and recently determined that the low level of tamoxifen N-oxide production in human liver microsomes may be explained by the kinetics of FMO1 versus FMO3.	tamoxifen N-oxide	91-108	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	194-198
16719388-3	2006	Studies with recombinant FMO enzymes demonstrate that FMOI and FMO3 are the primary catalysts of benzydamine N-oxygenation, with minimal contributions from cytochrome P450 enzymes.	benzydamine n	97-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
16719388-4	2006	Investigations conducted with human liver microsomes confirm that FMO3, in large part, is responsible for benzydamine N-oxide formation in this tissue.	benzydamine N-oxide	106-125	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
16719388-6	2006	In addition, benzydamine appears to be a suitable in vivo probe for human liver FMO3.	Benzydamine	13-24	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
16719389-2	2006	Prochiral sulfoxidation of probe compounds based on p-tolyl methyl sulfide is a particularly useful method for discriminating among FMO1, FMO3, and FMO5, because the stereochemistry of the resulting products is isoform dependent, but apparently species independent.	dimethyl sulfide	60-74	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
15564885-0	2004	Benzydamine metabolism in vivo is impaired in patients with deficiency of flavin-containing monooxygenase 3.	Benzydamine	0-11	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	74-107
15623613-0	2004	Genetic polymorphisms of human flavin monooxygenase 3 in sulindac-mediated primary chemoprevention of familial adenomatous polyposis.	Sulindac	57-65	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	31-53
15623613-3	2004	The present study determined whether polymorphisms in the gene encoding flavin monooxygenase 3 (FMO3), a hepatic microsomal enzyme that inactivates sulindac, played a role in determining the efficacy of sulindac in preventing polyposis in this cohort of FAP patients.	Sulindac	148-156	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-94
15623613-3	2004	The present study determined whether polymorphisms in the gene encoding flavin monooxygenase 3 (FMO3), a hepatic microsomal enzyme that inactivates sulindac, played a role in determining the efficacy of sulindac in preventing polyposis in this cohort of FAP patients.	Sulindac	148-156	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	96-100
15623613-3	2004	The present study determined whether polymorphisms in the gene encoding flavin monooxygenase 3 (FMO3), a hepatic microsomal enzyme that inactivates sulindac, played a role in determining the efficacy of sulindac in preventing polyposis in this cohort of FAP patients.	Sulindac	203-211	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-94
15623613-3	2004	The present study determined whether polymorphisms in the gene encoding flavin monooxygenase 3 (FMO3), a hepatic microsomal enzyme that inactivates sulindac, played a role in determining the efficacy of sulindac in preventing polyposis in this cohort of FAP patients.	Sulindac	203-211	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	96-100
15623613-4	2004	EXPERIMENTAL DESIGN: Genotyping was performed on seven established FMO3 polymorphisms previously shown to have functional relevance-M66I, P153L, E158K, V257M, E305X, E308G, and R492W-in 21 and 20 FAP patients, who received sulindac and placebo, respectively.	Sulindac	223-231	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	67-71
15623613-9	2004	CONCLUSIONS: Polymorphisms in FMO3, particularly at the E158K and E308G loci, may reduce activity in catabolizing sulindac and result in an increased efficacy to prevent polyposis in FAP.	Sulindac	114-122	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-34
15680226-3	2005	Previous work from this laboratory has shown l-methionine to be S-oxidized by rat, rabbit and human FMO1-4, with FMO3 exhibiting the highest stereoselectivity for the formation of the d-diastereomer of methionine sulfoxide.	Methionine	45-57	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-117
15680226-3	2005	Previous work from this laboratory has shown l-methionine to be S-oxidized by rat, rabbit and human FMO1-4, with FMO3 exhibiting the highest stereoselectivity for the formation of the d-diastereomer of methionine sulfoxide.	methionine sulfoxide	202-222	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-117
15680226-8	2005	With FMO3, the activity measured with methionine was similar (1 mM) or higher (5 mM) than the activity measured with H-Met-Val-OH and H-Met-Phe-OH.	Methionine	38-48	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	5-9
14976351-11	2004	FMO3 metabolized fenthion to its sulfoxide at a lower catalytic efficiency than FMO1 (27%) and with less stereoselectivity (74% (+)-sulfoxide).	Fenthion	17-25	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
15363661-5	2004	This hypothesis is based on the imbalance observed between the decrease in FMO3 expression (40.7% of controls) and FMO3-specific ranitidine N-oxidation activity (15.1%), and on the partial or complete reversibility of FMO inhibition by sulfhydryl-reducing regents such as DTT (effective on both S-S and S-NO adducts) and ascorbate (effective on S-NO only).	ranitidine n	129-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	115-119
15363661-6	2004	Furthermore, NO donors (SNP, SNAP, and Sin-1), including the pure NO donor DEA/NO, directly suppressed in vitro FMO activity (N- or S-oxidation of ranitidine, trimethylamine, and thiobenzamide) in human liver microsomal proteins and recombinant human FMO3.	dea	75-78	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	251-255
15352021-11	2004	Deprenyl enantiomers and S-methamphetamine were substrates of human recombinant FMO3.	Methamphetamine	25-42	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	80-84
14976351-11	2004	FMO3 metabolized fenthion to its sulfoxide at a lower catalytic efficiency than FMO1 (27%) and with less stereoselectivity (74% (+)-sulfoxide).	sulfoxide	33-42	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
14976351-11	2004	FMO3 metabolized fenthion to its sulfoxide at a lower catalytic efficiency than FMO1 (27%) and with less stereoselectivity (74% (+)-sulfoxide).	sulfoxide	128-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
14742144-10	2003	In contrast, methimazole was effective in suppressing the catalytic activity of recombinant human FMO1 and FMO3.	Methimazole	13-24	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	107-111
12678693-4	2003	The genetic variability of the flavin-containing monooxygenase (form 3) that is responsible for detoxication and deodoration of trimethylamine is discussed and put in context with other variant forms of the flavin-containing monooxygenase (forms 1-5).	trimethylamine	128-142	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	31-70
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	Methimazole	110-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	11-15
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	Methimazole	110-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	71-75
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	trimethylamine	123-137	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	11-15
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	trimethylamine	123-137	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	71-75
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine	142-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	11-15
12814961-11	2003	The His132-FMO3 variant moderately altered the catalytic efficiency of FMO3 (decrease of 30%, 60% and 6% with methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively).	10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine	142-203	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	71-75
12814961-13	2003	Pro360-FMO3 oxygenated methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively, 3-, 5- and 2-fold more efficiently than wild-type FMO3.	Methimazole	23-34	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-11
12814961-13	2003	Pro360-FMO3 oxygenated methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively, 3-, 5- and 2-fold more efficiently than wild-type FMO3.	Methimazole	23-34	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	182-186
12814961-13	2003	Pro360-FMO3 oxygenated methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively, 3-, 5- and 2-fold more efficiently than wild-type FMO3.	trimethylamine	36-50	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-11
12814961-13	2003	Pro360-FMO3 oxygenated methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively, 3-, 5- and 2-fold more efficiently than wild-type FMO3.	trimethylamine	36-50	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	182-186
12814961-13	2003	Pro360-FMO3 oxygenated methimazole, trimethylamine and 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine, respectively, 3-, 5- and 2-fold more efficiently than wild-type FMO3.	10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine	55-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	7-11
12695352-8	2003	Tolperisone inhibited methyl p-tolyl sulfide oxidation (K(i) = 1200 microM) in recombinant flavin-containing monooxygenase 3 (FMO3) and resulted in a 3-fold (p < 0.01) higher turnover number using rFMO3 than that of control microsomes.	Tolperisone	0-11	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	91-124
12695352-8	2003	Tolperisone inhibited methyl p-tolyl sulfide oxidation (K(i) = 1200 microM) in recombinant flavin-containing monooxygenase 3 (FMO3) and resulted in a 3-fold (p < 0.01) higher turnover number using rFMO3 than that of control microsomes.	Tolperisone	0-11	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	126-130
12695352-8	2003	Tolperisone inhibited methyl p-tolyl sulfide oxidation (K(i) = 1200 microM) in recombinant flavin-containing monooxygenase 3 (FMO3) and resulted in a 3-fold (p < 0.01) higher turnover number using rFMO3 than that of control microsomes.	methyl 4-tolylsulfide	22-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	91-124
12695352-8	2003	Tolperisone inhibited methyl p-tolyl sulfide oxidation (K(i) = 1200 microM) in recombinant flavin-containing monooxygenase 3 (FMO3) and resulted in a 3-fold (p < 0.01) higher turnover number using rFMO3 than that of control microsomes.	methyl 4-tolylsulfide	22-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	126-130
12214664-2	2002	The major FMO in adult human liver, FMO3, is responsible for trimethylamine (TMA) N-oxygenation.	trimethylamine	61-75	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	36-40
12504349-4	2003	Nicotine N-1-oxide formation is catalysed by hepatic flavin-containing monooxygenase form 3 (FMO3), but the enzyme(s) required for cotinine N-1"-oxide formation has not been identified.	nicotine 1-N-oxide	0-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	53-91
12504349-4	2003	Nicotine N-1-oxide formation is catalysed by hepatic flavin-containing monooxygenase form 3 (FMO3), but the enzyme(s) required for cotinine N-1"-oxide formation has not been identified.	nicotine 1-N-oxide	0-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	93-97
12504349-4	2003	Nicotine N-1-oxide formation is catalysed by hepatic flavin-containing monooxygenase form 3 (FMO3), but the enzyme(s) required for cotinine N-1"-oxide formation has not been identified.	cotinine n-1"-oxide	131-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	93-97
12228178-6	2002	Examples of such interindividual variation come from the study of very rare mutations of the human FMO3 gene that have been associated with deficient N-oxygenation of dietary trimethylamine.	Nitrogen	150-151	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
12228178-6	2002	Examples of such interindividual variation come from the study of very rare mutations of the human FMO3 gene that have been associated with deficient N-oxygenation of dietary trimethylamine.	trimethylamine	175-189	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
12228184-4	2002	The metabolism of benzydamine to its major metabolite, the N-oxide, is mediated by FMO3 in humans.	Benzydamine	18-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
12228184-4	2002	The metabolism of benzydamine to its major metabolite, the N-oxide, is mediated by FMO3 in humans.	n-oxide	59-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
12642475-9	2003	Upon incubation of tazarotenic acid with microsomes expressing CYP2C8, flavin-containing monooxygenase 1 (FMO1), or FMO3, marked formation of the sulfoxide metabolite was observed.	tazarotenic acid	19-35	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
12642475-9	2003	Upon incubation of tazarotenic acid with microsomes expressing CYP2C8, flavin-containing monooxygenase 1 (FMO1), or FMO3, marked formation of the sulfoxide metabolite was observed.	sulfoxide	146-155	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
12490590-2	2003	Incubations of human cDNA-expressed FMO1, FMO3, FMO4, and FMO5 with SAC resulted in detection of SAC sulfoxide, with FMO3 exhibiting approximately 3-, 4-, and 10-fold higher activity than FMO1, FMO4, and FMO5, respectively.	sulfoxide	101-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
12490590-3	2003	DCVC sulfoxide formation was only detected with FMO3 and was 59-fold lower than SAC sulfoxide formation.	S-(1,2-dichlorovinyl)-L-cysteine sulfoxide	0-14	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
12490590-3	2003	DCVC sulfoxide formation was only detected with FMO3 and was 59-fold lower than SAC sulfoxide formation.	sulfoxide	5-14	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
12490590-4	2003	Incubations of human liver microsomes with SAC or DCVC resulted in detection of the corresponding sulfoxides and provided evidence for the involvement of FMO3.	S-(1,2-dichlorovinyl)cysteine	50-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	154-158
11717182-1	2001	The N-oxygenation of amines by the human flavin-containing monooxygenase (form 3) (FMO3) represents an important means for the conversion of lipophilic nucleophilic heteroatom-containing compounds into more polar and readily excreted products.	Amines	21-27	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-81
12084621-4	2002	Three flavin monooxygenase isozymes (FMO1, FMO3, and FMO5) with NADPH are not active as assayed.	NADP	64-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-47
12052141-2	2002	Evidence for six forms of the FMO gene exist but it is FMO form 3 (FMO3) that is the prominent form in adult human liver that is likely to be associated with the bulk of FMO-mediated metabolism.	fmo	30-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-65
12052141-2	2002	Evidence for six forms of the FMO gene exist but it is FMO form 3 (FMO3) that is the prominent form in adult human liver that is likely to be associated with the bulk of FMO-mediated metabolism.	fmo	30-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	67-71
12052141-6	2002	Certain mutations of the human FMO3 gene have been associated with abnormal N-oxygenation of trimethylamine.	Nitrogen	76-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	31-35
12052141-6	2002	Certain mutations of the human FMO3 gene have been associated with abnormal N-oxygenation of trimethylamine.	trimethylamine	93-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	31-35
12130684-10	2002	Taking advantage of the high sequence identity between FMO3 and FMO6, it is posited that the loss of binding sites for the serine-arginine-rich splicing factor protein family within exons 3 and 4 contributes to the exon skipping events, although the most commonly observed alternative splice event results from a 21-bp insertion immediately 3" to the predicted FMO6 intron 8 splice acceptor site, diminishing the efficiency of this site.	Serine	123-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
12365199-0	2002	6-methylhydroxylation of the anti-cancer agent 5,6-dimethylxanthenone-4-acetic acid (DMXAA) by flavin-containing monooxygenase 3.	vadimezan	47-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-128
12365199-0	2002	6-methylhydroxylation of the anti-cancer agent 5,6-dimethylxanthenone-4-acetic acid (DMXAA) by flavin-containing monooxygenase 3.	vadimezan	85-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-128
12365199-3	2002	Only FMO3 formed 6-OH-MXAA at a similar rate to that in cDNA-expressed cytochromes P-450 (CYP)1A2.	6-oh-mxaa	17-26	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	5-9
12365199-4	2002	The results of this study indicate that human FMO3 has the capacity to form 6-OH-MXAA, but plays a lesser important role for this reaction than CYP1A2 that has been demonstrated to catalyse 6-OH-MXAA formation.	6-oh-mxaa	76-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
12365199-4	2002	The results of this study indicate that human FMO3 has the capacity to form 6-OH-MXAA, but plays a lesser important role for this reaction than CYP1A2 that has been demonstrated to catalyse 6-OH-MXAA formation.	6-oh-mxaa	190-199	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
11717182-1	2001	The N-oxygenation of amines by the human flavin-containing monooxygenase (form 3) (FMO3) represents an important means for the conversion of lipophilic nucleophilic heteroatom-containing compounds into more polar and readily excreted products.	Amines	21-27	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	83-87
11717182-3	2001	For example, abnormal N-oxygenation of trimethylamine has been shown to segregate with mutations of human FMO3.	Nitrogen	22-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
11717182-3	2001	For example, abnormal N-oxygenation of trimethylamine has been shown to segregate with mutations of human FMO3.	trimethylamine	39-53	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
11038163-13	2000	The apparent K(m) for N-oxide K11777 formation by cDNA-expressed FMO3 was 109 +/- 11 microM.	n-oxide	22-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	65-69
11414682-7	2001	Recombinant rat FMO3 showed activities of methimazole S-oxidation, and NADPH oxidation associated with the N- or S-oxidation of trimethylamine and thioacetamide, in good concordance with those reported for human FMO3.	Thioacetamide	147-160	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	212-216
11266081-0	2001	A novel deletion in the flavin-containing monooxygenase gene (FMO3) in a Greek patient with trimethylaminuria.	4,6-dinitro-o-cresol	24-30	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-66
11266081-1	2001	Mutations of the flavin-containing monooxygenase type 3 gene (FMO3) that encode the major functional form present in adult human liver, have been shown to cause trimethylaminuria.	4,6-dinitro-o-cresol	17-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-66
11266081-6	2001	For the proband homozygous for the human FMO3 gene deletion, it is predicted that in addition to loss of monooxygenase function for human FMO3 substrates, such as TMA and other amines, the proband will exhibit decreased tolerance of biogenic amines, both medicinal and those found in foods.	Amines	177-183	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
11266081-6	2001	For the proband homozygous for the human FMO3 gene deletion, it is predicted that in addition to loss of monooxygenase function for human FMO3 substrates, such as TMA and other amines, the proband will exhibit decreased tolerance of biogenic amines, both medicinal and those found in foods.	Amines	177-183	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
11266081-6	2001	For the proband homozygous for the human FMO3 gene deletion, it is predicted that in addition to loss of monooxygenase function for human FMO3 substrates, such as TMA and other amines, the proband will exhibit decreased tolerance of biogenic amines, both medicinal and those found in foods.	Amines	242-248	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
11266081-6	2001	For the proband homozygous for the human FMO3 gene deletion, it is predicted that in addition to loss of monooxygenase function for human FMO3 substrates, such as TMA and other amines, the proband will exhibit decreased tolerance of biogenic amines, both medicinal and those found in foods.	Amines	242-248	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
11136294-15	2000	CONCLUSIONS: BZD N-oxidation in human liver is mainly catalysed by FMO3 and enzyme activity is affected by FMO3 genotype.	bzd n	13-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	67-71
11136294-15	2000	CONCLUSIONS: BZD N-oxidation in human liver is mainly catalysed by FMO3 and enzyme activity is affected by FMO3 genotype.	bzd n	13-18	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	107-111
11191884-3	2000	Ordinarily, dietary-derived TMA is oxidized to the nonodorous N-oxide by hepatic flavin-containing monooxygenase 3 (FMO3).	trimethylamine	28-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	81-114
11191884-3	2000	Ordinarily, dietary-derived TMA is oxidized to the nonodorous N-oxide by hepatic flavin-containing monooxygenase 3 (FMO3).	trimethylamine	28-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
11191884-3	2000	Ordinarily, dietary-derived TMA is oxidized to the nonodorous N-oxide by hepatic flavin-containing monooxygenase 3 (FMO3).	n-oxide	62-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	81-114
11191884-3	2000	Ordinarily, dietary-derived TMA is oxidized to the nonodorous N-oxide by hepatic flavin-containing monooxygenase 3 (FMO3).	n-oxide	62-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
11191884-10	2000	Since an asparagine is conserved at the equivalent position to N61 of FMO3 in mammalian, yeast and Caenorhabditis elegans FMOs, the characterization of the naturally occurring N61S (A to G) mutation may have identified this asparagine as playing a critical role specifically in FMO-catalysed N-oxidation.	Asparagine	224-234	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
11191884-10	2000	Since an asparagine is conserved at the equivalent position to N61 of FMO3 in mammalian, yeast and Caenorhabditis elegans FMOs, the characterization of the naturally occurring N61S (A to G) mutation may have identified this asparagine as playing a critical role specifically in FMO-catalysed N-oxidation.	Nitrogen	63-64	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
11038163-14	2000	Based on the intrinsic formation clearances and the results of inhibition experiments (CYP2D6, 50 microM bufuralol; FMO3 mediated, 100 mM methionine) using human liver microsomes, it was estimated that CYP3A contributes to >80% of K11777 metabolite formation.	Methionine	138-148	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	116-120
11128045-3	2000	Recombinant FMO isozymes like FMO1, FMO2, FMO3 and FMO5 produced 39, 79, 2180 and 4 ranitinine N-oxide and 45, 0, 580 and 280 ranitinine S-oxide pmol x min(-1) x nmol(-1) FMO, respectively.	ranitinine n-oxide	84-102	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
11012553-7	2000	In contrast, benzydamine was a substrate for human FMO1, FMO3, FMO4 and FMO5.	Benzydamine	13-24	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
11012553-8	2000	Apparent Km values for benzydamine N-oxygenation were 60 +/- 8 microM, 80 +/- 8 microM, > 3 mM and > 2 mM, for FMO1, FMO3, FMO4 and FMO5, respectively.	Benzydamine	23-34	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	123-127
11012553-11	2000	CONCLUSIONS: FMO1 and FMO3 catalyse benzydamine N-oxygenation with the highest efficiency.	benzydamine n	36-49	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-26
11012553-12	2000	However, it is likely that the metabolic capacity of hepatic FMO3 is a much greater contributor to plasma levels of the N-oxide metabolite in vivo than is extrahepatic FMO1.	n-oxide	120-127	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
11012553-13	2000	Therefore, benzydamine, but not caffeine, is a potential in vivo probe for human FMO3.	Benzydamine	11-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	81-85
11128045-9	2000	Thus, urinary contents of ranitidine N-oxide can be used as the in vivo probe to determine the hepatic FMO3 activity.	ranitidine N-oxide	26-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	103-107
11128045-3	2000	Recombinant FMO isozymes like FMO1, FMO2, FMO3 and FMO5 produced 39, 79, 2180 and 4 ranitinine N-oxide and 45, 0, 580 and 280 ranitinine S-oxide pmol x min(-1) x nmol(-1) FMO, respectively.	ranitinine s-oxide	126-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	42-46
11128045-6	2000	FMO3, the major form in adult liver, produced both ranitidine N- and S-oxides at a 4 to 1 ratio.	ranitidine n- and s-oxides	51-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
11128045-7	2000	FMO1, expressed primarily in human kidney, was 55- and 13-fold less efficient than the hepatic FMO3 in producing ranitidine N- and S-oxides, respectively.	ranitidine n- and s-oxides	113-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-99
10898113-1	2000	We have previously shown that primary trimethylaminuria, or fish-odour syndrome, is caused by an inherited defect in the flavin-containing monooxygenase 3 (FMO3) catalysed N-oxidation of the dietary-derived malodorous amine, trimethylamine (TMA).	malodorous amine	207-223	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
11465082-4	2000	Both human FMO1 and FMO3 S-oxygenate a number of nucleophilic sulfur-containing substrates and in some cases, does so with great stereoselectivity.	Sulfur	62-68	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	20-24
11465082-5	2000	Human FMO3 is sensitive to steric features of the substrate and aliphatic amines with linkages between the nitrogen atom and a large aromatic group such as a phenothiazine of at least five carbons are N-oxygenated significantly more efficiently than those substrates with two or three carbons.	Amines	74-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-5	2000	Human FMO3 is sensitive to steric features of the substrate and aliphatic amines with linkages between the nitrogen atom and a large aromatic group such as a phenothiazine of at least five carbons are N-oxygenated significantly more efficiently than those substrates with two or three carbons.	Nitrogen	107-115	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-5	2000	Human FMO3 is sensitive to steric features of the substrate and aliphatic amines with linkages between the nitrogen atom and a large aromatic group such as a phenothiazine of at least five carbons are N-oxygenated significantly more efficiently than those substrates with two or three carbons.	phenothiazine	158-171	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-5	2000	Human FMO3 is sensitive to steric features of the substrate and aliphatic amines with linkages between the nitrogen atom and a large aromatic group such as a phenothiazine of at least five carbons are N-oxygenated significantly more efficiently than those substrates with two or three carbons.	Carbon	189-196	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-5	2000	Human FMO3 is sensitive to steric features of the substrate and aliphatic amines with linkages between the nitrogen atom and a large aromatic group such as a phenothiazine of at least five carbons are N-oxygenated significantly more efficiently than those substrates with two or three carbons.	Carbon	285-292	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-6	2000	For amines with smaller aromatic substituents such as phenethylamines, often these compounds are efficiently N-oxygenated by human FMO3.	Amines	4-10	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
11465082-6	2000	For amines with smaller aromatic substituents such as phenethylamines, often these compounds are efficiently N-oxygenated by human FMO3.	Phenethylamines	54-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	131-135
11465082-7	2000	Currently, the most promising non-invasive probe of in vivo human FMO3 functional activity is the formation of trimethylamine N-oxide from trimethylamine that comes from dietary choline.	trimethyloxamine	111-133	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
11465082-7	2000	Currently, the most promising non-invasive probe of in vivo human FMO3 functional activity is the formation of trimethylamine N-oxide from trimethylamine that comes from dietary choline.	trimethylamine	111-125	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
11465082-7	2000	Currently, the most promising non-invasive probe of in vivo human FMO3 functional activity is the formation of trimethylamine N-oxide from trimethylamine that comes from dietary choline.	Choline	178-185	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
11465082-8	2000	(S)-Nicotine N-1"-oxide formation can also be used as a highly stereoselective probe of human FMO3 function for adult humans that smoke cigarettes.	nicotine 1-N-oxide	0-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	94-98
11465082-9	2000	Finally, cimetidine S-oxygenation or ranitidine N-oxidation can also be used as a functional probe of human FMO3.	Cimetidine	9-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	108-112
10807940-5	2000	In human liver and flavin-containing monooxygenase 3 (FMO3) the V(max) for R-sulindac sulfoxide increased 60-70% at pH = 8.5, but for S-sulindac sulfoxide was unchanged.	r-sulindac sulfoxide	75-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	19-52
10807940-5	2000	In human liver and flavin-containing monooxygenase 3 (FMO3) the V(max) for R-sulindac sulfoxide increased 60-70% at pH = 8.5, but for S-sulindac sulfoxide was unchanged.	r-sulindac sulfoxide	75-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
10807940-5	2000	In human liver and flavin-containing monooxygenase 3 (FMO3) the V(max) for R-sulindac sulfoxide increased 60-70% at pH = 8.5, but for S-sulindac sulfoxide was unchanged.	Sulindac	134-154	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	54-58
10807940-12	2000	Purified mini-pig liver FMO1, rabbit lung FMO2, and human cDNA-expressed FMO3 efficiently oxidized sulindac sulfide with a high degree of stereoselectivity towards the R-isomer, but FMO5 lacked catalytic activity.	sulindac sulfide	99-115	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	73-77
11465082-3	2000	Human FMO3 N-oxygenates primary, secondary and tertiary amines whereas human FMO1 is only highly efficient at N-oxygenating tertiary amines.	Nitrogen	11-12	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-3	2000	Human FMO3 N-oxygenates primary, secondary and tertiary amines whereas human FMO1 is only highly efficient at N-oxygenating tertiary amines.	Amines	56-62	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11465082-3	2000	Human FMO3 N-oxygenates primary, secondary and tertiary amines whereas human FMO1 is only highly efficient at N-oxygenating tertiary amines.	Amines	133-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
11026737-0	2000	Cytochrome P-450 enzymes and FMO3 contribute to the disposition of the antipsychotic drug perazine in vitro.	Perazine	90-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-33
11026737-10	2000	Perazine-N-oxidation was mainly mediated by FMO3.	Perazine	0-8	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	44-48
11026737-14	2000	CONCLUSIONS: Alterations in the activity of CYP3A4, CYP2C9 and FMO3 through genetic polymorphisms, enzyme induction or inhibition bear the potential to cause clinically significant changes in perazine clearance.	Perazine	192-200	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	63-67
10898113-1	2000	We have previously shown that primary trimethylaminuria, or fish-odour syndrome, is caused by an inherited defect in the flavin-containing monooxygenase 3 (FMO3) catalysed N-oxidation of the dietary-derived malodorous amine, trimethylamine (TMA).	trimethylamine	225-239	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
10640514-3	2000	For example, the tertiary amine trimethylamine is N-oxygenated by human FMO3 to trimethylamine N-oxide, and trimethylamine N-oxide is excreted in a detoxication and deoderation process.	Amines	26-31	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10640514-3	2000	For example, the tertiary amine trimethylamine is N-oxygenated by human FMO3 to trimethylamine N-oxide, and trimethylamine N-oxide is excreted in a detoxication and deoderation process.	trimethylamine	32-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10640514-3	2000	For example, the tertiary amine trimethylamine is N-oxygenated by human FMO3 to trimethylamine N-oxide, and trimethylamine N-oxide is excreted in a detoxication and deoderation process.	trimethyloxamine	80-102	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10640514-9	2000	In vitro analysis of wild-type and variant human FMO3 proteins expressed from the cDNA for the two naturally occurring polymorphisms showed differences in substrate affinities for nitrogen-containing substrates.	Nitrogen	180-188	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	49-53
10640514-10	2000	Thus, for polymorphic forms of human FMO3, lower k(cat)/K(m) values for N-oxygenation of 10-(N, N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine, trimethylamine, and tyramine were observed.	Nitrogen	72-73	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
10640514-10	2000	Thus, for polymorphic forms of human FMO3, lower k(cat)/K(m) values for N-oxygenation of 10-(N, N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine, trimethylamine, and tyramine were observed.	10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine	89-152	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
10640514-10	2000	Thus, for polymorphic forms of human FMO3, lower k(cat)/K(m) values for N-oxygenation of 10-(N, N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine, trimethylamine, and tyramine were observed.	trimethylamine	154-168	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
10640514-10	2000	Thus, for polymorphic forms of human FMO3, lower k(cat)/K(m) values for N-oxygenation of 10-(N, N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine, trimethylamine, and tyramine were observed.	Tyramine	174-182	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
10640514-12	2000	The results imply that prevalent polymorphisms of the human FMO3 gene may contribute to low penetrance predispositions to diseases associated with adverse environmental exposures to heteroatom-containing chemicals, drugs, and endogenous amines.	Amines	237-243	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	60-64
10739174-11	2000	Therefore, we concluded that presence of FMO3/Lys158 and FMO3/Gly308 mutant alleles in FMO3 gene is responsible for the low ranitidine N-oxidation (FMO3 activity) in our Korean population.	Ranitidine	124-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-45
10739174-11	2000	Therefore, we concluded that presence of FMO3/Lys158 and FMO3/Gly308 mutant alleles in FMO3 gene is responsible for the low ranitidine N-oxidation (FMO3 activity) in our Korean population.	Ranitidine	124-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
10739174-11	2000	Therefore, we concluded that presence of FMO3/Lys158 and FMO3/Gly308 mutant alleles in FMO3 gene is responsible for the low ranitidine N-oxidation (FMO3 activity) in our Korean population.	Ranitidine	124-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
10739174-11	2000	Therefore, we concluded that presence of FMO3/Lys158 and FMO3/Gly308 mutant alleles in FMO3 gene is responsible for the low ranitidine N-oxidation (FMO3 activity) in our Korean population.	Ranitidine	124-134	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
10630426-1	2000	The Km value for tamoxifen is 1.2 mM for mouse FMO1 (human FMO1 is not expressed in adults) and 1.4 mM for human FMO3, with no detectable activity being expressed toward tamoxifen by FMO5 from either mouse or human.	Tamoxifen	17-26	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	113-117
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Arginine	14-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-99
10509757-0	1999	In vitro and in vivo inhibition of human flavin-containing monooxygenase form 3 (FMO3) in the presence of dietary indoles.	Indoles	114-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	41-79
10509757-0	1999	In vitro and in vivo inhibition of human flavin-containing monooxygenase form 3 (FMO3) in the presence of dietary indoles.	Indoles	114-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	81-85
10443982-6	1999	RESULTS: We confirmed by HPLC-mass spectrometry that MeDDC sulfine was the major product of MeDDC formed by human liver microsomes and by FMO3.	S-methyl-N,N-diethyldithiocarbamate sulfine	53-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	138-142
10443982-7	1999	Recombinant FMO3 was an efficient catalyst for the formation of MeDDC sulfine (5.3+/-0.2 nmol/min/mg, mean+/-SEM, n = 6).	S-methyl-N,N-diethyldithiocarbamate sulfine	64-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	12-16
10443982-10	1999	CONCLUSIONS: Our results prove that MeDDC sulfine is the major product of MeDDC oxidation in human liver microsomes, MeDDC is a good substrate for human FMO3, and MeDDC is metabolized in human liver microsomes primarily by CYP450.	S-methyl-N,N-diethyldithiocarbamate sulfine	36-49	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	153-157
10659950-15	2000	In human, metabolism of L-775,606 to the principal metabolites, M1 and M2, was mediated primarily by CYP3A4 with minimal contribution from CYP2C8, whereas the minor N-oxidative pathway was catalysed mainly by FMO3.	l-775	24-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	209-213
10546928-0	1999	Flavin monooxygenase 3 (FMO3) polymorphism in a white population: allele frequencies, mutation linkage, and functional effects on clozapine and caffeine metabolism.	Clozapine	130-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	24-28
10546928-0	1999	Flavin monooxygenase 3 (FMO3) polymorphism in a white population: allele frequencies, mutation linkage, and functional effects on clozapine and caffeine metabolism.	Caffeine	144-152	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	24-28
10546928-3	1999	We therefore wanted to analyze population frequencies and allelic linkage of FMO3 mutations and their functional effect on the metabolism of clozapine and caffeine.	Clozapine	141-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-81
10546928-3	1999	We therefore wanted to analyze population frequencies and allelic linkage of FMO3 mutations and their functional effect on the metabolism of clozapine and caffeine.	Caffeine	155-163	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-81
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Arginine	14-22	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	101-105
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Imipramine	110-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-99
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Imipramine	110-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	101-105
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Chlorpromazine	125-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	77-99
10445381-0	1999	The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine.	Chlorpromazine	125-139	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	101-105
10445381-1	1999	This study was carried out to investigate the molecular basis for modulation of recombinant FMO3-catalyzed activity by the tricyclic antidepressants, imipramine and chlorpromazine.	Imipramine	150-160	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	92-96
10445381-1	1999	This study was carried out to investigate the molecular basis for modulation of recombinant FMO3-catalyzed activity by the tricyclic antidepressants, imipramine and chlorpromazine.	Chlorpromazine	165-179	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	92-96
10445381-3	1999	Functional properties of native and T428R human FMO3s were studied with methimazole as substrate.	Methimazole	72-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
10445381-5	1999	Imipramine modulated the activities of the native and T428R human FMO3s differently; the activity of the native FMO3 was increased at all concentrations, whereas the activity of the mutant enzyme was inhibited at concentrations above 300 microM.	Imipramine	0-10	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
10445381-5	1999	Imipramine modulated the activities of the native and T428R human FMO3s differently; the activity of the native FMO3 was increased at all concentrations, whereas the activity of the mutant enzyme was inhibited at concentrations above 300 microM.	Imipramine	0-10	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	112-116
10376762-16	1999	Thus, individuals with these FMO3 gene mutations may have defective metabolic activity for many clinically used drugs and dietary plant alkaloids which are oxidized primarily by hepatic FMO3.	Alkaloids	136-145	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	29-33
10376762-16	1999	Thus, individuals with these FMO3 gene mutations may have defective metabolic activity for many clinically used drugs and dietary plant alkaloids which are oxidized primarily by hepatic FMO3.	Alkaloids	136-145	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	186-190
9840430-12	1998	By combining the results of the current study and those reported in the literature, it is proposed that CYP3A4 and FMO3 are primarily responsible for the production of clozapine N-oxide, and CYP3A4 and CYP1A2 are primarily responsible for the formation of N-desmethylclozapine.	norclozapine	256-276	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	115-119
10027866-0	1999	N-oxygenation of amphetamine and methamphetamine by the human flavin-containing monooxygenase (form 3): role in bioactivation and detoxication.	Amphetamine	17-28	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-101
10027866-0	1999	N-oxygenation of amphetamine and methamphetamine by the human flavin-containing monooxygenase (form 3): role in bioactivation and detoxication.	Methamphetamine	33-48	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-101
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	3-azido-2,7-naphthalene disulfonate	0-8	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-135
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	3-azido-2,7-naphthalene disulfonate	0-8	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Amphetamine	9-24	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-135
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Amphetamine	9-24	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Methamphetamine	29-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-135
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Methamphetamine	29-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Hydroxylamines	164-178	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-135
10027866-1	1999	(+)- And (-)-amphetamine and methamphetamine were N-oxygenated by the cDNA expressed adult human flavin-containing monooxygenase form 3 (FMO3), their corresponding hydroxylamines.	Hydroxylamines	164-178	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
10027866-2	1999	Two major polymorphic forms of human FMO3 were studied, and the results suggested preferential N-oxygenation by only one of the two enzymes.	Nitrogen	95-96	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	37-41
10027866-3	1999	Chemically synthesized (+/-)-amphetamine hydroxylamine was also a substrate for the human FMO3 and it was converted to phenylpropanone oxime with a stereoselectivity ratio of trans/cis of 5:1.	amphetamine hydroxylamine	23-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-94
10027866-3	1999	Chemically synthesized (+/-)-amphetamine hydroxylamine was also a substrate for the human FMO3 and it was converted to phenylpropanone oxime with a stereoselectivity ratio of trans/cis of 5:1.	phenylpropanone oxime	119-140	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-94
10027866-4	1999	Human FMO3 also N-oxygenated methamphetamine to produce methamphetamine hydroxylamine.	Methamphetamine	29-44	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
10027866-4	1999	Human FMO3 also N-oxygenated methamphetamine to produce methamphetamine hydroxylamine.	methamphetamine hydroxylamine	56-85	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
10027866-5	1999	Methamphetamine hydroxylamine was also N-oxygenated by human FMO3, and the ultimate product observed was phenylpropanone.	methamphetamine hydroxylamine	0-29	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
10027866-5	1999	Methamphetamine hydroxylamine was also N-oxygenated by human FMO3, and the ultimate product observed was phenylpropanone.	phenylpropanone	105-120	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	61-65
10027866-7	1999	This was supported by the observation that alpha-deutero (+/-)-amphetamine hydroxylamine gave an inverse kinetic isotope effect on product formation in the presence of human FMO3.	alpha-deutero (+/-)-amphetamine hydroxylamine	43-88	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-178
10027866-8	1999	For methamphetamine, the data were consistent with a mechanism of human FMO3-mediated N,N-dioxygenation but the immediate product, a nitrone, rapidly hydrolyzed to phenylpropanone.	Methamphetamine	4-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10027866-8	1999	For methamphetamine, the data were consistent with a mechanism of human FMO3-mediated N,N-dioxygenation but the immediate product, a nitrone, rapidly hydrolyzed to phenylpropanone.	Nitrogen	86-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10027866-8	1999	For methamphetamine, the data were consistent with a mechanism of human FMO3-mediated N,N-dioxygenation but the immediate product, a nitrone, rapidly hydrolyzed to phenylpropanone.	Nitrogen	88-89	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	72-76
10027866-12	1999	Because of the potential toxic nature of amphetamine hydroxylamine and methamphetamine hydroxylamine metabolites and the polymorphic nature of N-oxygenation, human FMO3-mediated metabolism of amphetamine or methamphetamine may have clinical consequences.	amphetamine hydroxylamine	41-66	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	164-168
10027866-12	1999	Because of the potential toxic nature of amphetamine hydroxylamine and methamphetamine hydroxylamine metabolites and the polymorphic nature of N-oxygenation, human FMO3-mediated metabolism of amphetamine or methamphetamine may have clinical consequences.	methamphetamine hydroxylamine	71-100	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	164-168
10027866-12	1999	Because of the potential toxic nature of amphetamine hydroxylamine and methamphetamine hydroxylamine metabolites and the polymorphic nature of N-oxygenation, human FMO3-mediated metabolism of amphetamine or methamphetamine may have clinical consequences.	Nitrogen	143-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	164-168
10027866-12	1999	Because of the potential toxic nature of amphetamine hydroxylamine and methamphetamine hydroxylamine metabolites and the polymorphic nature of N-oxygenation, human FMO3-mediated metabolism of amphetamine or methamphetamine may have clinical consequences.	Amphetamine	41-52	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	164-168
10027866-12	1999	Because of the potential toxic nature of amphetamine hydroxylamine and methamphetamine hydroxylamine metabolites and the polymorphic nature of N-oxygenation, human FMO3-mediated metabolism of amphetamine or methamphetamine may have clinical consequences.	Methamphetamine	71-86	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	164-168
10215790-0	1999	Sequence variations in the flavin-containing mono-oxygenase 3 gene (FMO3) in fish odour syndrome.	4,6-dinitro-o-cresol	27-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-72
10215790-2	1999	Flavin-containing mono-oxygenase 3 (FMO3) catalyses TMA oxidation and mutations in the FMO3 gene have recently been shown to underlie trimethylaminuria/fish odour syndrome.	4,6-dinitro-o-cresol	0-6	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	36-40
10215790-2	1999	Flavin-containing mono-oxygenase 3 (FMO3) catalyses TMA oxidation and mutations in the FMO3 gene have recently been shown to underlie trimethylaminuria/fish odour syndrome.	4,6-dinitro-o-cresol	0-6	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	87-91
9840430-3	1998	In vitro metabolism of clozapine was investigated using human CYP1A1, CYP1A2, CYP2C8, CYP2E1, CYP2C9-arg144, CYP2C9-cys144, CYP2C19, CYP2D6, CYP3A4, CYP3A5 and FMO3 supplemented with an NADPH generating system.	Clozapine	23-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	160-164
9840430-12	1998	By combining the results of the current study and those reported in the literature, it is proposed that CYP3A4 and FMO3 are primarily responsible for the production of clozapine N-oxide, and CYP3A4 and CYP1A2 are primarily responsible for the formation of N-desmethylclozapine.	clozapine N-oxide	168-185	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	115-119
9750169-2	1998	Imipramine activates FMO3-catalyzed metabolism of methimazole at all substrate concentrations tested.	Imipramine	0-10	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	21-25
9776311-3	1998	Human FMO3 was by far the most active isoform, exhibiting a turnover number of 30 nmol TMAO/nmol FMO3/min at pH 7.4 and 0.5 mM TMA.	trimethyloxamine	87-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
9776311-3	1998	Human FMO3 was by far the most active isoform, exhibiting a turnover number of 30 nmol TMAO/nmol FMO3/min at pH 7.4 and 0.5 mM TMA.	trimethyloxamine	87-91	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-101
9776311-3	1998	Human FMO3 was by far the most active isoform, exhibiting a turnover number of 30 nmol TMAO/nmol FMO3/min at pH 7.4 and 0.5 mM TMA.	trimethylamine	87-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	6-10
9776311-3	1998	Human FMO3 was by far the most active isoform, exhibiting a turnover number of 30 nmol TMAO/nmol FMO3/min at pH 7.4 and 0.5 mM TMA.	trimethylamine	87-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	97-101
9776311-6	1998	Kinetic studies of TMAO formation by recombinant human FMO3, employing three different analytical methods, resulted in a Km of 28 +/- 1 microM and a Vmax of 36.3 +/- 5.7 nmol TMAO/nmol FMO3/min.	trimethyloxamine	19-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
9776311-6	1998	Kinetic studies of TMAO formation by recombinant human FMO3, employing three different analytical methods, resulted in a Km of 28 +/- 1 microM and a Vmax of 36.3 +/- 5.7 nmol TMAO/nmol FMO3/min.	trimethyloxamine	19-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	185-189
9776311-6	1998	Kinetic studies of TMAO formation by recombinant human FMO3, employing three different analytical methods, resulted in a Km of 28 +/- 1 microM and a Vmax of 36.3 +/- 5.7 nmol TMAO/nmol FMO3/min.	trimethyloxamine	175-179	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
9776311-8	1998	Therefore, at physiological pH, human FMO3 is a very specific and efficient TMA N-oxygenase, and is likely responsible for the metabolic clearance of TMA in vivo in humans.	trimethylamine	76-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	38-42
9776311-9	1998	In addition, this specificity provides a good in vitro probe for the determination of FMO3-mediated activity in human tissues, by analyzing TMAO formation at pH 7.4 with TMA concentrations not higher than 0.5 mM.	trimethyloxamine	140-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	86-90
9776311-9	1998	In addition, this specificity provides a good in vitro probe for the determination of FMO3-mediated activity in human tissues, by analyzing TMAO formation at pH 7.4 with TMA concentrations not higher than 0.5 mM.	trimethylamine	140-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	86-90
9750169-10	1998	Our findings show that the activity of FMO3 can be modulated by large drug molecules as well as short-chain amines and metal ions.	Amines	108-114	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	39-43
9776311-0	1998	Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes: selective catalysis by FMO3.	trimethylamine n	23-39	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	140-144
9750169-10	1998	Our findings show that the activity of FMO3 can be modulated by large drug molecules as well as short-chain amines and metal ions.	Metals	119-124	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	39-43
9750169-2	1998	Imipramine activates FMO3-catalyzed metabolism of methimazole at all substrate concentrations tested.	Methimazole	50-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	21-25
9750169-4	1998	The response of FMO3 is also unique in that chlorpromazine is markedly more effective as a modulator than is imipramine.	Chlorpromazine	44-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
9750169-4	1998	The response of FMO3 is also unique in that chlorpromazine is markedly more effective as a modulator than is imipramine.	Imipramine	109-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
9750169-5	1998	n-Octylamine, MgCl2, and HgCl2 all inhibit FMO3, the first two in a biphasic manner.	octylamine	0-12	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-47
9750169-5	1998	n-Octylamine, MgCl2, and HgCl2 all inhibit FMO3, the first two in a biphasic manner.	Magnesium Chloride	14-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-47
9750169-5	1998	n-Octylamine, MgCl2, and HgCl2 all inhibit FMO3, the first two in a biphasic manner.	Mercuric Chloride	25-30	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	43-47
9536088-0	1998	Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication.	4,6-dinitro-o-cresol	17-23	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
9536088-2	1998	We show here that mutations in the human flavin-containing monooxygenase isoform 3 gene ( FMO3 ) impair N -oxygenation of xenobiotics and are responsible for the trimethylaminuria phenotype.	4,6-dinitro-o-cresol	41-47	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-94
9536088-2	1998	We show here that mutations in the human flavin-containing monooxygenase isoform 3 gene ( FMO3 ) impair N -oxygenation of xenobiotics and are responsible for the trimethylaminuria phenotype.	Nitrogen	104-105	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	90-94
9536088-5	1998	These findings illustrate the critical role played by human FMO3 in the metabolism of xenobiotic substrates and endogenous amines.	Amines	123-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	60-64
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	Glycyrrhizic Acid	74-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
9398858-3	1997	TMA oxidation is catalyzed by flavin-containing mono-oxygenase (FMO; refs 7,8), and tissue localization and functional studies have established FMO3 as the form most likely to be defective in fish-odour syndrome.	4,6-dinitro-o-cresol	30-36	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-148
9344459-8	1997	Catalytic activities of mouse and human FMO3 were high toward the substrate methimazole; however, in the presence of trimethylamine and thioacetamide, FMO-dependent methimazole oxidation by both enzymes was reduced by greater than 85%.	Methimazole	76-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
9344459-8	1997	Catalytic activities of mouse and human FMO3 were high toward the substrate methimazole; however, in the presence of trimethylamine and thioacetamide, FMO-dependent methimazole oxidation by both enzymes was reduced by greater than 85%.	trimethylamine	117-131	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
9344459-8	1997	Catalytic activities of mouse and human FMO3 were high toward the substrate methimazole; however, in the presence of trimethylamine and thioacetamide, FMO-dependent methimazole oxidation by both enzymes was reduced by greater than 85%.	Thioacetamide	136-149	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
9344459-8	1997	Catalytic activities of mouse and human FMO3 were high toward the substrate methimazole; however, in the presence of trimethylamine and thioacetamide, FMO-dependent methimazole oxidation by both enzymes was reduced by greater than 85%.	Methimazole	165-176	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	40-44
9282831-7	1997	The variant human FMO3 cDNA was constructed from wild type human FMO3 cDNA by site-directed mutagenesis as maltose-binding protein fusions.	Maltose	107-114	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	18-22
9282831-8	1997	Five distinct human FMO3 mutants were expressed as fusion proteins in Escherichia coli and compared with wild type human FMO3 maltose-binding proteins (FMO3-MBP) for the N-oxygenation of 10-[(N,N-dimethylamino)pentyl]-2-(trifluoromethyl)phenothiazine, tyramine, and trimethylamine.	Maltose	126-133	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	121-125
9282831-8	1997	Five distinct human FMO3 mutants were expressed as fusion proteins in Escherichia coli and compared with wild type human FMO3 maltose-binding proteins (FMO3-MBP) for the N-oxygenation of 10-[(N,N-dimethylamino)pentyl]-2-(trifluoromethyl)phenothiazine, tyramine, and trimethylamine.	10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl) phenothiazine	187-250	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	121-125
9282832-4	1997	The conclusion that FMO was predominantly responsible for trans oxime formation in human liver microsomes was based on the effect of incubation conditions on tyramine N-oxygenation and the observation that cDNA-expressed human FMO3 also N-oxygenated tyramine to give exclusively the trans oxime.	trans oxime	58-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	227-231
9282832-4	1997	The conclusion that FMO was predominantly responsible for trans oxime formation in human liver microsomes was based on the effect of incubation conditions on tyramine N-oxygenation and the observation that cDNA-expressed human FMO3 also N-oxygenated tyramine to give exclusively the trans oxime.	Tyramine	250-258	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	227-231
9282832-4	1997	The conclusion that FMO was predominantly responsible for trans oxime formation in human liver microsomes was based on the effect of incubation conditions on tyramine N-oxygenation and the observation that cDNA-expressed human FMO3 also N-oxygenated tyramine to give exclusively the trans oxime.	trans oxime	283-294	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	227-231
9282832-7	1997	The results suggested that tyramine was sequentially N-oxygenated in the presence of pig and human liver microsomes and cDNA-expressed FMO3 to the hydroxylamine and then to the di-N-hydroxylamine that was spontaneously dehydrated to the trans oxime.	Tyramine	27-35	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	135-139
9282832-7	1997	The results suggested that tyramine was sequentially N-oxygenated in the presence of pig and human liver microsomes and cDNA-expressed FMO3 to the hydroxylamine and then to the di-N-hydroxylamine that was spontaneously dehydrated to the trans oxime.	Hydroxylamine	147-160	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	135-139
9282832-7	1997	The results suggested that tyramine was sequentially N-oxygenated in the presence of pig and human liver microsomes and cDNA-expressed FMO3 to the hydroxylamine and then to the di-N-hydroxylamine that was spontaneously dehydrated to the trans oxime.	di-n-hydroxylamine	177-195	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	135-139
9282832-7	1997	The results suggested that tyramine was sequentially N-oxygenated in the presence of pig and human liver microsomes and cDNA-expressed FMO3 to the hydroxylamine and then to the di-N-hydroxylamine that was spontaneously dehydrated to the trans oxime.	trans oxime	237-248	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	135-139
8902275-0	1996	N-oxygenation of primary amines and hydroxylamines and retroreduction of hydroxylamines by adult human liver microsomes and adult human flavin-containing monooxygenase 3.	Nitrogen	0-1	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	136-169
8902275-0	1996	N-oxygenation of primary amines and hydroxylamines and retroreduction of hydroxylamines by adult human liver microsomes and adult human flavin-containing monooxygenase 3.	Hydroxylamines	73-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	136-169
8902275-4	1996	Studies on the biochemical mechanism of oxime formation suggested that cis-oxime formation in the presence of adult human liver microsomes was largely dependent on the human flavin-containing monooxygenase (form 3).	Oximes	40-45	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-213
8902275-4	1996	Studies on the biochemical mechanism of oxime formation suggested that cis-oxime formation in the presence of adult human liver microsomes was largely dependent on the human flavin-containing monooxygenase (form 3).	cis-oxime	71-80	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	174-213
8632334-8	1996	N-O olanzapine formation correlated with human liver flavin-containing monooxygenase (FMO3) levels and activity.	n-o olanzapine	0-14	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	53-90
8632334-10	1996	These results suggest that CYP1A2 catalyzes NdM olanzapine and 7-OH olanzapine formation, CYP2D6 catalyzes 2-OH olanzapine formation and FMO3 catalyzes N-O olanzapine formation.	ndm olanzapine	44-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
8632334-10	1996	These results suggest that CYP1A2 catalyzes NdM olanzapine and 7-OH olanzapine formation, CYP2D6 catalyzes 2-OH olanzapine formation and FMO3 catalyzes N-O olanzapine formation.	7-oh olanzapine	63-78	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
8632334-10	1996	These results suggest that CYP1A2 catalyzes NdM olanzapine and 7-OH olanzapine formation, CYP2D6 catalyzes 2-OH olanzapine formation and FMO3 catalyzes N-O olanzapine formation.	n-o olanzapine	152-166	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	137-141
7720101-12	1995	FMO1 and FMO3, expressed in either system, displayed product stereoselectivity in their catalysis of the N-oxidation of the pro-chiral tertiary amines, N-ethyl-N-methylaniline (EMA) and pargyline.	Amines	144-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
7720101-12	1995	FMO1 and FMO3, expressed in either system, displayed product stereoselectivity in their catalysis of the N-oxidation of the pro-chiral tertiary amines, N-ethyl-N-methylaniline (EMA) and pargyline.	N-ethyl-N-methylaniline	152-175	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
7720101-12	1995	FMO1 and FMO3, expressed in either system, displayed product stereoselectivity in their catalysis of the N-oxidation of the pro-chiral tertiary amines, N-ethyl-N-methylaniline (EMA) and pargyline.	N-ethyl-N-methylaniline	177-180	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
7720101-12	1995	FMO1 and FMO3, expressed in either system, displayed product stereoselectivity in their catalysis of the N-oxidation of the pro-chiral tertiary amines, N-ethyl-N-methylaniline (EMA) and pargyline.	Pargyline	186-195	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	9-13
7720101-14	1995	But in the case of pargyline, the enzymes displayed opposite stereoselectivity, FMO1 producing solely the (+)-enantiomer and FMO3 predominantly the (-)-enantiomer of the N-oxide.	Pargyline	19-28	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	125-129
7720101-14	1995	But in the case of pargyline, the enzymes displayed opposite stereoselectivity, FMO1 producing solely the (+)-enantiomer and FMO3 predominantly the (-)-enantiomer of the N-oxide.	n-oxide	170-177	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	125-129
7720103-4	1995	In both cases, the majority of evidence points to adult human liver FMO3 as the principal enzyme responsible for cimetidine S-oxygenation and (S)-nicotine N-1"-oxygenation in vitro and in vivo.	Cimetidine	113-123	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-72
7720103-4	1995	In both cases, the majority of evidence points to adult human liver FMO3 as the principal enzyme responsible for cimetidine S-oxygenation and (S)-nicotine N-1"-oxygenation in vitro and in vivo.	Nicotine	142-154	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	68-72
7720103-6	1995	Further, that adult human liver cDNA-expressed FMO3 in Escherichia coli also gave the same absolute stereoselectivity (i.e. for (S)-nicotine N-1"-oxygenation) confirms the identity of the monoxygenase in vivo.	Nicotine	128-140	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
8128486-10	1994	In contrast, (S)-nicotine is oxidized by human FMO3 exclusively to the trans-N-1"-oxide.	Nicotine	13-25	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
8128486-10	1994	In contrast, (S)-nicotine is oxidized by human FMO3 exclusively to the trans-N-1"-oxide.	trans-n-1"-oxide	71-87	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	47-51
34265522-1	2021	Screening inhibitors of flavin monooxygenase 3 (FMO3) is very important for treating trimethylamine N-oxide (TMAO) derived thrombotic diseases.	trimethyloxamine	85-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
34265522-1	2021	Screening inhibitors of flavin monooxygenase 3 (FMO3) is very important for treating trimethylamine N-oxide (TMAO) derived thrombotic diseases.	trimethyloxamine	109-113	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	48-52
34265522-3	2021	To this end, the optimized supramolecular host-guest (p-sulfonatocalix(4)arene-oxazine 1) reporter pair and FMO3 catalytic system were exploited to determine the influence of the bioactive compounds in XFZYD on the conversion from TMA to TMAO.	trimethyloxamine	238-242	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	108-112
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	naringin	32-40	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	peoniflorin	42-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	20-HYDROXYECDYSONE	56-72	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
9305407-1	1997	Variable amounts of flavin-containing monooxygenase isoforms 3 and 5 (FMO3 and FMO5) are present in microsomal preparations from adult, male, human liver.	4,6-dinitro-o-cresol	20-26	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	70-74
9305407-6	1997	This conclusion was supported by several lines of evidence: first, the catalytic efficiency of FMO3 with methimazole was found to be approximately 5000 times greater than that of FMO5; second, the rate of metabolism showed a direct, quantitative relationship with FMO3 content; third, the plot of the relationship between metabolism and FMO3 content extrapolated close to the origin.	Methimazole	105-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	95-99
9305407-6	1997	This conclusion was supported by several lines of evidence: first, the catalytic efficiency of FMO3 with methimazole was found to be approximately 5000 times greater than that of FMO5; second, the rate of metabolism showed a direct, quantitative relationship with FMO3 content; third, the plot of the relationship between metabolism and FMO3 content extrapolated close to the origin.	Methimazole	105-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	264-268
9305407-6	1997	This conclusion was supported by several lines of evidence: first, the catalytic efficiency of FMO3 with methimazole was found to be approximately 5000 times greater than that of FMO5; second, the rate of metabolism showed a direct, quantitative relationship with FMO3 content; third, the plot of the relationship between metabolism and FMO3 content extrapolated close to the origin.	Methimazole	105-116	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	264-268
9305407-7	1997	A second reaction, the N-oxidation of ranitidine, exhibited a much higher Km with recombinant FMO3 than did methimazole (2 mM vs. 35 microM).	Ranitidine	38-48	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	94-98
9280409-0	1997	Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions.	Maltose	112-119	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-69
9280409-6	1997	It was found that expression of both lys158 and glu158 enzymes of the human flavin-containing monooxygenase form 3 as fusions with the maltose binding protein resulted in an enzyme that was soluble and greatly stabilized and had a reduced requirement for detergent during enzyme purification and during the assay for activity.	Maltose	135-142	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-114
9280409-8	1997	With the exception of the stability and solubility characteristics, the physical and chemical properties of lys158 and glu158 maltose binding fusion proteins of human flavin-containing monooxygenase form 3 variants resembled that of flavin-containing monooxygenase enzyme activity associated with human liver microsomes and enzyme isolated from a previous Escherichia coli expression system that lacked the protein fusion.	Maltose	126-133	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	167-205
9280409-10	1997	Expression of the adult human flavin-containing monooxygenase form 3 as a maltose binding protein has allowed considerable advances over the previously reported cDNA-expressed enzyme systems and may provide the basis for examining the role of the flavin-containing monooxygenase in human xenobiotic or drug metabolism.	Maltose	74-81	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	30-68
9224773-3	1997	Sulfoxidation of the methyl and ethyl p-tolyl sulfides by recombinant human FMO3 proceeded with little stereochemical preference, whereas sulfoxidation of the n-propyl and n-butyl homologs demonstrated increasing selectivity for formation of the (R)-sulfoxide.	methyl and ethyl p-tolyl sulfides	21-54	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
9224773-3	1997	Sulfoxidation of the methyl and ethyl p-tolyl sulfides by recombinant human FMO3 proceeded with little stereochemical preference, whereas sulfoxidation of the n-propyl and n-butyl homologs demonstrated increasing selectivity for formation of the (R)-sulfoxide.	(r)-sulfoxide	246-259	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	76-80
9224773-5	1997	Catalytically active human FMO3 was purified to apparent homogeneity by cholate solubilization and sequential column chromatography on Octyl-Sepharose, DEAE-Sepharose, and hydroxyapatite.	Cholates	72-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
9224773-5	1997	Catalytically active human FMO3 was purified to apparent homogeneity by cholate solubilization and sequential column chromatography on Octyl-Sepharose, DEAE-Sepharose, and hydroxyapatite.	octyl-sepharose CL-4B	135-150	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
9224773-5	1997	Catalytically active human FMO3 was purified to apparent homogeneity by cholate solubilization and sequential column chromatography on Octyl-Sepharose, DEAE-Sepharose, and hydroxyapatite.	deae-sepharose	152-166	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
9224773-5	1997	Catalytically active human FMO3 was purified to apparent homogeneity by cholate solubilization and sequential column chromatography on Octyl-Sepharose, DEAE-Sepharose, and hydroxyapatite.	Durapatite	172-186	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
9224773-8	1997	LC/electrospray-mass spectrometry analysis of purified FMO3 identified >70% of the tryptic peptides, including fragments containing motifs for N-linked glycosylation and O-linked glycosylation.	Peptides	94-102	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
9224773-10	1997	Edman degradation of the recombinant product revealed that posttranslational modification of human FMO3 by insect cells was limited to cleavage at the N-terminal methionine, a process seen in vivo with animal orthologs of FMO3.	Methionine	162-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	99-103
9224773-10	1997	Edman degradation of the recombinant product revealed that posttranslational modification of human FMO3 by insect cells was limited to cleavage at the N-terminal methionine, a process seen in vivo with animal orthologs of FMO3.	Methionine	162-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	222-226
9107553-3	1997	Also the Michaelis-Menten kinetic constant; KM determined for CLZ N-oxidation catalyzed by purified human FMO3 (324 microM) was very similar to the mean value obtained in these laboratories for the microsomal preparations of seven human livers.	clz n	62-67	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	106-110
8117918-3	1993	The cDNA-expressed FMO3 was used to investigate the regio- and stereoselective N- and S-oxygenation of a number of tertiary amines and sulfides, respectively.	Nitrogen	6-7	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	19-23
8117918-3	1993	The cDNA-expressed FMO3 was used to investigate the regio- and stereoselective N- and S-oxygenation of a number of tertiary amines and sulfides, respectively.	tertiary amines	115-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	19-23
8117918-3	1993	The cDNA-expressed FMO3 was used to investigate the regio- and stereoselective N- and S-oxygenation of a number of tertiary amines and sulfides, respectively.	Sulfides	135-143	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	19-23
8117918-5	1993	Both cDNA-expressed FMO3 and adult human liver microsomes N-oxygenated trifluoperazine or 10-(N,N-dimethylaminoalkyl)-phenothiazines with similar substrate specificities.	Trifluoperazine	71-86	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	20-24
8117918-5	1993	Both cDNA-expressed FMO3 and adult human liver microsomes N-oxygenated trifluoperazine or 10-(N,N-dimethylaminoalkyl)-phenothiazines with similar substrate specificities.	10-(n,n-dimethylaminoalkyl)-phenothiazines	90-132	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	20-24
8117918-7	1993	Nucleophilic sulfur-containing compounds [i.e., thiobenzamide, (4-bromophenyl)-1,3-oxathiolane, and 2-methyl-1,3-benzodithiole] were efficiently S-oxygenated by cDNA-expressed FMO3 and adult human liver microsomes.	Sulfur	13-19	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
8117918-7	1993	Nucleophilic sulfur-containing compounds [i.e., thiobenzamide, (4-bromophenyl)-1,3-oxathiolane, and 2-methyl-1,3-benzodithiole] were efficiently S-oxygenated by cDNA-expressed FMO3 and adult human liver microsomes.	thiobenzamide	48-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
8117918-7	1993	Nucleophilic sulfur-containing compounds [i.e., thiobenzamide, (4-bromophenyl)-1,3-oxathiolane, and 2-methyl-1,3-benzodithiole] were efficiently S-oxygenated by cDNA-expressed FMO3 and adult human liver microsomes.	(4-bromophenyl)-1,3-oxathiolane	63-94	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
8117918-7	1993	Nucleophilic sulfur-containing compounds [i.e., thiobenzamide, (4-bromophenyl)-1,3-oxathiolane, and 2-methyl-1,3-benzodithiole] were efficiently S-oxygenated by cDNA-expressed FMO3 and adult human liver microsomes.	1,3-Benzodithiole, 2-methyl-	100-126	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	176-180
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	Amygdalin	100-109	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	albiflorin	111-121	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
34265522-4	2021	From the nine compounds tested, naringin, paeoniflorin, beta-ecdysterone, 18beta-glycyrrhizic acid, amygdalin, albiflorin, and saikosaponin A downregulated FMO3 activity and reduced TMAO biosynthesis.	saikosaponin D	127-141	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	156-160
34265522-5	2021	Moreover, molecular docking was successfully applied to simulate the optimal conformation of a receptor-ligand complex between FMO3 and all tested compounds except for beta-ecdysterone.	20-HYDROXYECDYSONE	168-184	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	127-131
34611047-6	2022	TMA then enters the liver through the portal vein circulation and is oxidised to trimethylamine oxide (TMAO) by the hepatic flavin-containing mono-oxygenase (FMO) family, especially FMO3.	trimethyloxamine	81-101	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	182-186
34509493-8	2021	This behaviour is different from hFMO3, that is shown to form both H2O2 and superoxide anion radical as a result of ~50% uncoupling.	Hydrogen Peroxide	67-71	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	33-38
34509493-8	2021	This behaviour is different from hFMO3, that is shown to form both H2O2 and superoxide anion radical as a result of ~50% uncoupling.	Superoxides	76-100	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	33-38
34611047-6	2022	TMA then enters the liver through the portal vein circulation and is oxidised to trimethylamine oxide (TMAO) by the hepatic flavin-containing mono-oxygenase (FMO) family, especially FMO3.	trimethyloxamine	103-107	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	182-186
34611047-6	2022	TMA then enters the liver through the portal vein circulation and is oxidised to trimethylamine oxide (TMAO) by the hepatic flavin-containing mono-oxygenase (FMO) family, especially FMO3.	4,6-dinitro-o-cresol	124-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	182-186
34841334-2	2021	TMA is further oxidized to trimethylamine-N-oxide (TMAO), by the liver enzyme flavin-dependent monooxygenase 3 (FMO3).	trimethyloxamine	27-49	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	78-110
34352706-1	2021	The predicted contributions of flavin-containing monooxygenase 3 (FMO3) to drug candidate N-oxygenations can be estimated using classic base dissociation constants of the N-containing moiety.	Nitrogen	171-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	31-64
34352706-1	2021	The predicted contributions of flavin-containing monooxygenase 3 (FMO3) to drug candidate N-oxygenations can be estimated using classic base dissociation constants of the N-containing moiety.	Nitrogen	171-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	66-70
34352706-7	2021	This method, along with in silico pKa (base) values > 8.4, could prove useful for predicting the contributions of FMO3 to N-oxygenations as part of drug development.	Nitrogen	122-123	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	114-118
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethylamine	127-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	56-60
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethylamine	127-130	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-84
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethylamine	132-146	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	56-60
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethylamine	132-146	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-84
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethyloxamine	151-173	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	56-60
34597008-2	2021	The condition is caused by a homozygous mutation in the FMO3 (flavin monooxygenase 3) gene coding for the enzyme that converts TMA (trimethylamine) to trimethylamine N-oxide.	trimethyloxamine	151-173	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	62-84
34512362-0	2021	Influence of FMO3 and CYP3A4 Polymorphisms on the Pharmacokinetics of Teneligliptin in Humans.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	70-83	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	13-17
34512362-2	2021	FMO3 and CYP3A4 metabolize teneligliptin into teneligliptin sulfoxide.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	27-40	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
34512362-2	2021	FMO3 and CYP3A4 metabolize teneligliptin into teneligliptin sulfoxide.	teneligliptin sulfoxide	46-69	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	0-4
34512362-6	2021	These results suggest that FMO3 and CYP3A4 polymorphisms affect teneligliptin pharmacokinetics in humans.	3-(4-(4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl)pyrrolidin-2-ylcarbonyl)thiazolidine	64-77	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	27-31
34159537-8	2022	The FMO3 rs2266782 polymorphism was associated with the plasma TMAO concentrations in our cohort, and lower TMAO levels were found in the AA-genotype.	trimethyloxamine	63-67	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-8
34159537-8	2022	The FMO3 rs2266782 polymorphism was associated with the plasma TMAO concentrations in our cohort, and lower TMAO levels were found in the AA-genotype.	trimethyloxamine	108-112	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	4-8
34159537-9	2022	Thus, higher plasma TMAO levels indicated increased risk of the composite outcome of cardiovascular death or heart transplantation independent of potential confounders, and the FMO3 AA-genotype in rs2266782 was related to lower plasma TMAO levels.	trimethyloxamine	235-239	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	177-181
34841334-2	2021	TMA is further oxidized to trimethylamine-N-oxide (TMAO), by the liver enzyme flavin-dependent monooxygenase 3 (FMO3).	trimethyloxamine	27-49	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	112-116
34841334-2	2021	TMA is further oxidized to trimethylamine-N-oxide (TMAO), by the liver enzyme flavin-dependent monooxygenase 3 (FMO3).	trimethyloxamine	51-55	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	78-110
34841334-2	2021	TMA is further oxidized to trimethylamine-N-oxide (TMAO), by the liver enzyme flavin-dependent monooxygenase 3 (FMO3).	trimethyloxamine	51-55	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	112-116
35129779-8	2022	Not only does CYP3A4, flavin-containing monooxygenase 3 (FMO3), and uridine 5"-diphospho-glucuronosyltransferase (UGT) also metabolize dasatinib, and similarly, by glucuronidation process, asciminib gets metabolized by UGT enzymes (UGT1A3, UGT1A4, UGT2B7, and UGT2B17).	Dasatinib	135-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	22-55
35129779-8	2022	Not only does CYP3A4, flavin-containing monooxygenase 3 (FMO3), and uridine 5"-diphospho-glucuronosyltransferase (UGT) also metabolize dasatinib, and similarly, by glucuronidation process, asciminib gets metabolized by UGT enzymes (UGT1A3, UGT1A4, UGT2B7, and UGT2B17).	Dasatinib	135-144	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	57-61
35065293-2	2022	The conversion of TMA to TMAO is mainly catalyzed by flavin-containing monooxygenases 3 (FMO3) and FMO1.	trimethylamine	18-21	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	53-87
35348964-0	2022	Possible correlation between high circulatory levels of trimethylamine-N-oxide and 2177G>C polymorphisms of hepatic flavin containing monooxygenase 3 in Kurdish Population with non-alcoholic fatty liver disease.	trimethyloxamine	56-78	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	108-149
35348964-3	2022	The single nucleotide polymorphisms (SNPs) of hepatic flavin-containing monooxygenase 3 (FMO3) regulate the concentration of TMAO.	trimethyloxamine	125-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-87
35348964-3	2022	The single nucleotide polymorphisms (SNPs) of hepatic flavin-containing monooxygenase 3 (FMO3) regulate the concentration of TMAO.	trimethyloxamine	125-129	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-93
35348964-11	2022	CONCLUSIONS: The current results provide documentation for high circulatory levels of TMAO and its possible correlation with the presence of the specific genotype -2177G>C FMO3 in Kurdish NAFLD patients.	trimethyloxamine	86-90	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	172-176
35065293-2	2022	The conversion of TMA to TMAO is mainly catalyzed by flavin-containing monooxygenases 3 (FMO3) and FMO1.	trimethylamine	18-21	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	89-93
33247860-1	2021	WHAT IS KNOWN AND OBJECTIVE: Trimethylaminuria is a metabolic disorder characterized by excessive excretion of trimethylamine in body fluids following FMO3 gene mutations.	trimethylamine	111-125	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	151-155
35084335-8	2022	We show the gut microbial choline metabolite trimethylamine (TMA) is elevated in AH patients and correlates with reduced hepatic expression of the TMA oxygenase flavin-containing monooxygenase 3 (FMO3).	Choline	26-33	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
35084335-8	2022	We show the gut microbial choline metabolite trimethylamine (TMA) is elevated in AH patients and correlates with reduced hepatic expression of the TMA oxygenase flavin-containing monooxygenase 3 (FMO3).	trimethylamine	45-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	196-200
33831674-1	2021	The oxygenation of food-derived trimethylamine to its N-oxide is a representative reaction mediated by human flavin-containing monooxygenase 3 (FMO3).	trimethylamine	32-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	109-142
33831674-1	2021	The oxygenation of food-derived trimethylamine to its N-oxide is a representative reaction mediated by human flavin-containing monooxygenase 3 (FMO3).	trimethylamine	32-46	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-148
33831674-1	2021	The oxygenation of food-derived trimethylamine to its N-oxide is a representative reaction mediated by human flavin-containing monooxygenase 3 (FMO3).	n-oxide	54-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	109-142
33831674-1	2021	The oxygenation of food-derived trimethylamine to its N-oxide is a representative reaction mediated by human flavin-containing monooxygenase 3 (FMO3).	n-oxide	54-61	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	144-148
33831674-8	2021	Although the present novel mutations or alleles were relatively rare, both in self-reported Japanese trimethylaminuria sufferers and in the genomic database panel, three common FMO3 missense or deletion variants severely impaired FMO3-mediated N-oxygenation of trimethylamine.	trimethylamine	261-275	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	177-181
33831674-8	2021	Although the present novel mutations or alleles were relatively rare, both in self-reported Japanese trimethylaminuria sufferers and in the genomic database panel, three common FMO3 missense or deletion variants severely impaired FMO3-mediated N-oxygenation of trimethylamine.	trimethylamine	261-275	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	230-234
33709384-5	2021	TMA is formed by intestinal microbial metabolism of choline and L-carnitine and converted into TMAO by FMO3.	trimethyloxamine	95-99	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	103-107
33533968-3	2021	TMAO production results from the fermentation by the gut microbiota of dietary nutrients such as choline and carnitine, which are transformed to trimethylamine (TMA) and converted into TMAO in the liver by flavin-containing monooxygenase 1 and 3 (FMO1 and FMO3).	trimethyloxamine	0-4	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	256-260
33089397-0	2021	Association of FMO3 rs1736557 polymorphism with clopidogrel response in Chinese patients with coronary artery disease.	Clopidogrel	48-59	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	15-19
33089397-5	2021	This study aimed to explore the association between FMO3 rs1736557 polymorphism and clopidogrel response.	Clopidogrel	84-95	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	52-56
33089397-12	2021	CONCLUSION: The FMO3 rs1736557 AA genotype was related to an increased the antiplatelet potency of clopidogrel in Chinese CAD patients.	Clopidogrel	99-110	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	16-20
33746664-3	2021	It is formed by the process of oxidation of trimethylamine (TMA) by the hepatic flavin monooxygenases (FMO1 and FMO3).	trimethylamine	44-58	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	112-116
33533968-3	2021	TMAO production results from the fermentation by the gut microbiota of dietary nutrients such as choline and carnitine, which are transformed to trimethylamine (TMA) and converted into TMAO in the liver by flavin-containing monooxygenase 1 and 3 (FMO1 and FMO3).	Choline	97-104	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	256-260
33533968-3	2021	TMAO production results from the fermentation by the gut microbiota of dietary nutrients such as choline and carnitine, which are transformed to trimethylamine (TMA) and converted into TMAO in the liver by flavin-containing monooxygenase 1 and 3 (FMO1 and FMO3).	Carnitine	109-118	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	256-260
33533968-3	2021	TMAO production results from the fermentation by the gut microbiota of dietary nutrients such as choline and carnitine, which are transformed to trimethylamine (TMA) and converted into TMAO in the liver by flavin-containing monooxygenase 1 and 3 (FMO1 and FMO3).	trimethyloxamine	185-189	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	256-260
33288187-5	2020	Multiple clinical and experimental evidences suggested that dietary fatty acids (FAs) can affect TMAO production through gut microbiota and/or FMO3 enzyme activity.	Fatty Acids	68-79	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	143-147
32998136-0	2021	Predictive Value of FMO3 Variants on Plasma Disposition and Adverse Reactions of Oral Voriconazole in Febrile Neutropenia.	Voriconazole	86-98	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	20-24
32998136-2	2021	The study was designed for evaluating the influence of FMO3 mutation on the plasma disposition and adverse reactions of VRC in FN.	Voriconazole	120-123	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	55-59
32998136-10	2021	Moreover, patients with the FMO3 E308G genotype were more likely to have adverse drug reactions and abnormal serum parameters after receiving VRC treatment.	Voriconazole	142-145	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	28-32
32998136-11	2021	For example, the serum potassium level in the FMO3 E308G genotype group was significantly lower than that in the WT group (p = 0.028), the abnormal level of total bilirubin in the FMO3 E308G genotype group was significantly higher than that in the WT group (p = 0.049), and the aspartate aminotransferase level in the E308G group was significantly higher than that in the WT group (p = 0.05).	Potassium	23-32	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
32998136-11	2021	For example, the serum potassium level in the FMO3 E308G genotype group was significantly lower than that in the WT group (p = 0.028), the abnormal level of total bilirubin in the FMO3 E308G genotype group was significantly higher than that in the WT group (p = 0.049), and the aspartate aminotransferase level in the E308G group was significantly higher than that in the WT group (p = 0.05).	Bilirubin	163-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	46-50
32998136-11	2021	For example, the serum potassium level in the FMO3 E308G genotype group was significantly lower than that in the WT group (p = 0.028), the abnormal level of total bilirubin in the FMO3 E308G genotype group was significantly higher than that in the WT group (p = 0.049), and the aspartate aminotransferase level in the E308G group was significantly higher than that in the WT group (p = 0.05).	Bilirubin	163-172	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	180-184
33288187-5	2020	Multiple clinical and experimental evidences suggested that dietary fatty acids (FAs) can affect TMAO production through gut microbiota and/or FMO3 enzyme activity.	Fatty Acids	81-84	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	143-147