EC 1.14.13.8 - Flavin-containing monooxygenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.14.13.8

Names

Accepted name:
flavin-containing monooxygenase
Other names:
N,N-dimethylaniline monooxygenase
DMA oxidase
FAD-containing monooxygenase
FMO
FMO-I
FMO-II
dimethylaniline N-oxidase
dimethylaniline oxidase
flavin monooxygenase
mixed-function amine oxidase
flavin mixed function oxidase
Ziegler's enzyme
FMO1
FMO2
FMO3
FMO4
FMO5
methylphenyltetrahydropyridine N-monooxygenase
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase
dimethylaniline monooxygenase (N-oxide-forming)
Systematic name:
N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)

Reaction

Cofactor

Comments:

A flavoprotein. 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 [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme 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) [2,6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004499
CAS Registry Number: 37256-73-8
UniProtKB/Swiss-Prot: (34) [show] [UniProt]

References

  1. Ziegler, D.M. and Pettit, F.H.
    Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes.
    Biochemistry 5: 2932-2938 (1966). [PMID: 4381353]
  2. Chiba, K., Kubota, E., Miyakawa, T., Kato, Y. and Ishizaki, T.
    Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice.
    J. Pharmacol. Exp. Ther. 246: 1108-1115 (1988). [PMID: 3262153]
  3. Cashman, J.R.
    Structural and catalytic properties of the mammalian flavin-containing monooxygenase.
    Chem. Res. Toxicol. 8: 165-181 (1995).
  4. Cashman, J.R. and Zhang, J.
    Human flavin-containing monooxygenases.
    Annu. Rev. Pharmacol. Toxicol. 46: 65-100 (2006). [PMID: 16402899]
  5. Jones, K.C. and Ballou, D.P.
    Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates.
    J. Biol. Chem. 261: 2553-2559 (1986). [PMID: 3949735]
  6. Chiba, K., Kobayashi, K., Itoh, K., Itoh, S., Chiba, T., Ishizaki, T. and Kamataki, T.
    N-oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells.
    Eur. J. Pharmacol. 293: 97-100 (1995). [PMID: 7672012]

[EC 1.14.13.8 created 1972 (EC 1.13.12.11 created 1992, part-incorporated 2006), modified 2006]