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ENZYME entry: EC

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.
Methylphenyltetrahydropyridine N-monooxygenase.
Mixed-function amine oxidase.
N,N-dimethylaniline monooxygenase.
Ziegler's enzyme.
Reaction catalysed
N,N-dimethylaniline + NADPH + O(2) <=> N,N-dimethylaniline N-oxide + NADP(+) + H(2)O
  • 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
PRIAM enzyme-specific profiles1.14.13.8
KEGG Ligand Database for Enzyme Nomenclature1.14.13.8
IUBMB Enzyme Nomenclature1.14.13.8
MEDLINEFind literature relating to
Q95LA2, FMO1_CANLF;  P49328, FMO1_CAVPO;  Q01740, FMO1_HUMAN;  
P50285, FMO1_MOUSE;  P16549, FMO1_PIG;  P17636, FMO1_RABIT;  
P36365, FMO1_RAT;  P36366, FMO2_CAVPO;  Q8HZ69, FMO2_GORGO;  
Q99518, FMO2_HUMAN;  Q28505, FMO2_MACMU;  Q8K2I3, FMO2_MOUSE;  
P31513, FMO3_HUMAN;  Q8SPQ7, FMO3_MACMU;  P97501, FMO3_MOUSE;  
Q7YS44, FMO3_PANTR;  P32417, FMO3_RABIT;  Q9EQ76, FMO3_RAT;  
P31512, FMO4_HUMAN;  Q8VHG0, FMO4_MOUSE;  P36367, FMO4_RABIT;  
Q8K4B7, FMO4_RAT;  P49109, FMO5_CAVPO;  P49326, FMO5_HUMAN;  
P97872, FMO5_MOUSE;  Q04799, FMO5_RABIT;  Q8K4C0, FMO5_RAT;  
O60774, FMO6_HUMAN;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.13.-
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