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

Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)

N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]

R03344;
(other) R04523 R05623 R08266

N,N-dimethylaniline [CPD:C02846];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]

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]

1  [PMID:4381353]

Ziegler DM, Pettit FH.

Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes.

Biochemistry. 5 (1966) 2932-8.

Sus scofa [GN:ssc]

2  [PMID:3262153]

Chiba K, Kubota E, Miyakawa T, Kato Y, 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 (1988) 1108-15.

3

Cashman, J.R.

Structural and catalytic properties of the mammalian flavin-containing monooxygenase.

Chem. Res. Toxicol. 8 (1995) 165-181.

4  [PMID:16402899]

Cashman JR, Zhang J.

Human flavin-containing monooxygenases.

Annu. Rev. Pharmacol. Toxicol. 46 (2006) 65-100.

Homo sapiens [GN:hsa]

5  [PMID:3949735]

Jones KC, Ballou DP.

Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates.

J. Biol. Chem. 261 (1986) 2553-9.

Sus scofa [GN:ssc]

6  [PMID:7672012]

Chiba K, Kobayashi K, Itoh K, Itoh S, Chiba T, Ishizaki T, 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 (1995) 97-100.

Rattus norvegicus [GN:rno]