PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
15680226-8	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	
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	
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