PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15352021-10	2004	FMO1, the extrahepatic form of the enzyme in man, was shown to be more active in the N-oxygenation of both deprenyl and methamphetamine isomers than FMO3.	Nitrogen	85-86	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	0-4	
11725960-8	2001	In addition, microsomes containing cDNA-expressed FMO1, a major isoform in human kidney, mainly catalyzed N-oxidation of SNI-2011, but microsomes containing FMO3, a major isoform in adult human liver, did not.	Nitrogen	37-38	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	50-54	
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 1	Homo sapiens	77-81	
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 1	Homo sapiens	63-67	
20642449-7	2010	Quinuclidine oxidation was another pathway of importance, yielding an N-oxide (M12) which was also observed in all species.P450 2D6 and FMO1 catalyze the oxidation of the quinuclidine nitrogen.	Nitrogen	184-192	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	136-140	
14976351-0	2004	Evaluation of xenobiotic N- and S-oxidation by variant flavin-containing monooxygenase 1 (FMO1) enzymes.	Nitrogen	25-26	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	55-88	
14976351-0	2004	Evaluation of xenobiotic N- and S-oxidation by variant flavin-containing monooxygenase 1 (FMO1) enzymes.	Nitrogen	25-26	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	90-94