PMID:22006322

Chen Y, Patel NA, Crombie A, Scrivens JH, Murrell JC

Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase.

Proc Natl Acad Sci U S A 108:17791-6 (2011)
DOI:10.1073/pnas.1112928108

[msl:Msil_3604]

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

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

N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O [RN:R05623]

R05623
Reaction

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

A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].

EC 1.14.13.148 created 2012

1  [PMID:4404764]

Large PJ, Boulton CA, Crabbe MJ

The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans.

Biochem J 128:137P-138P (1972)
DOI:10.1042/bj1280137pb

2  [PMID:9417913]

Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR

Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA.

Genomics 46:260-7 (1997)
DOI:10.1006/geno.1997.5031

[hsa:2328]

3  [PMID:9536088]

Treacy EP, Akerman BR, Chow LM, Youil R, Bibeau C, Lin J, Bruce AG, Knight M, Danks DM, Cashman JR, Forrest SM

Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication.

Hum Mol Genet 7:839-45 (1998)
DOI:10.1093/hmg/7.5.839

[rno:84493]

4  [PMID:22006322]

Chen Y, Patel NA, Crombie A, Scrivens JH, Murrell JC

Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase.

Proc Natl Acad Sci U S A 108:17791-6 (2011)
DOI:10.1073/pnas.1112928108

[msl:Msil_3604]