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ENZYME

ENZYME entry: EC 1.14.13.8

Accepted Name
flavin-containing monooxygenase
Alternative Name(s)
dimethylaniline monooxygenase (N-oxide-forming)
dimethylaniline N-oxidase
dimethylaniline oxidase
DMA oxidase
FAD-containing monooxygenase
flavin mixed function oxidase
flavin monooxygenase
FMO
methylphenyltetrahydropyridine N-monooxygenase
mixed-function amine oxidase
N,N-dimethylaniline monooxygenase
Ziegler's enzyme
Reaction catalysed
H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+)
Comment(s)
  • A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines.
  • Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate.
  • Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites.
  • For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl- 1,2,3,6-tetrahydropyridine (MPTP).
  • Formerly EC 1.13.12.11.
Cross-references
BRENDA1.14.13.8
EC2PDB1.14.13.8
ExplorEnz1.14.13.8
PRIAM enzyme-specific profiles1.14.13.8
KEGG Ligand Database for Enzyme Nomenclature1.14.13.8
IUBMB Enzyme Nomenclature1.14.13.8
IntEnz1.14.13.8
MEDLINEFind literature relating to 1.14.13.8
MetaCyc1.14.13.8
Rhea expert-curated reactions1.14.13.8
UniProtKB/Swiss-Prot
Q95LA2, FMO1_CANLFQ01740, FMO1_HUMANP50285, FMO1_MOUSE
P16549, FMO1_PIGP17636, FMO1_RABITP36365, FMO1_RAT
Q28505, FMO2_MACMUP17635, FMO2_RABITQ8HYJ9, FMO3_BOVIN
Q95LA1, FMO3_CANLFP49328, FMO3_CAVPOP31513, FMO3_HUMAN
Q8SPQ7, FMO3_MACMUP97501, FMO3_MOUSEQ7YS44, FMO3_PANTR
P32417, FMO3_RABITQ9EQ76, FMO3_RATP31512, FMO4_HUMAN
Q8VHG0, FMO4_MOUSEP36367, FMO4_RABITQ8K4B7, FMO4_RAT
P49109, FMO5_CAVPOP49326, FMO5_HUMANP97872, FMO5_MOUSE
Q04799, FMO5_RABITQ8K4C0, FMO5_RATO60774, FMO6_HUMAN

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