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Literature summary for 1.14.13.8 extracted from

  • Lang, D.H.; Yeung, C.K.; Peter, R.M.; Ibarra, C.; Gasser, R.; Itagaki, K.; Philpot, R.M.; Rettie, A.E.
    Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes: selective catalysis by FMO3 (1998), Biochem. Pharmacol., 56, 1005-1012.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Trichoplusia ni cells using a baculovirus expression vector system Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q01740
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver adult liver Homo sapiens
-
additional information no activity in fetal human liver, intestine, and kidney Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform FMO5 exhibits a low catalytic activity only for sulfoxidation of methyl 4-tolyl sulfide Homo sapiens ?
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
-
Homo sapiens N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
flavin-containing monooxygenase
-
Homo sapiens
FMO1 isoform Homo sapiens
FMO4 isoform Homo sapiens
FMO5 isoform Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
NADPH required for activity Homo sapiens