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Literature summary extracted from

  • Siddens, L.K.; Krueger, S.K.; Henderson, M.C.; Williams, D.E.
    Mammalian flavin-containing monooxygenase (FMO) as a source of hydrogen peroxide (2014), Biochem. Pharmacol., 89, 141-147 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.8 expressed in Sf9 insect cell microsomes Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.8 N413K the mutant of isoform FMO2 exhibits higher catalytic activity toward methyl-4-tolyl sulfide compared to the wild type enzyme Homo sapiens
1.14.13.8 S195L the mutant of isoform FMO2 exhibits lower catalytic activity toward methyl-4-tolyl sulfide and ethylene thiourea compared to the wild type enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.8 liver
-
 Homo sapiens
-
1.14.13.8 lung
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 ethylene thiourea + NADPH + H+ + O2
-
 Homo sapiens ?
-
 ?
1.14.13.8 methyl-4-tolyl sulfide + NADPH + H+ + O2
-
 Homo sapiens ?
-
 ?
1.14.13.8 trimethylamine + NADPH + H+ + O2 substrate of isoform FMO3 Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.8 FMO1 isoform Homo sapiens
1.14.13.8 FMO2 isoform Homo sapiens
1.14.13.8 FMO3 isoform Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.8 FAD
-
 Homo sapiens
1.14.13.8 NADPH
-
 Homo sapiens