PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
11012553-13	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
17142560-7	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	
17142560-8	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	
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	
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