Trimethylamine monooxygenase

Trimethylamine monooxygenase
Identifiers
EC number	1.14.13.148
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Trimethylamine monooxygenase (EC 1.14.13.148, flavin-containing monooxygenase 3, FMO3, tmm (gene)) is an enzyme with systematic name N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming).^[1][2][3][4] This enzyme catalyses the following chemical reaction

N,N,N-trimethylamine + NADPH + H⁺ + O₂ $\rightleftharpoons$ N,N,N-trimethylamine N-oxide + NADP⁺ + H₂O

Trimethylamine monooxygenase is a flavoprotein.

References

1. Large, P.J., Boulton, C.A. and Crabbe, M.J. (1972). "The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans". Biochem. J. 128 (4): 137P–138P. PMC 1173958. PMID 4404764.
2. Dolphin, C.T., Riley, J.H., Smith, R.L., Shephard, E.A. and Phillips, I.R. (1997). "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: 260–267. doi:10.1006/geno.1997.5031. PMID 9417913.
3. Treacy, E.P., Akerman, B.R., Chow, L.M., Youil, R., Bibeau, C., Lin, J., Bruce, A.G., Knight, M., Danks, D.M., Cashman, J.R. and Forrest, S.M. (1998). "Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication". Hum. Mol. Genet. 7: 839–845. doi:10.1093/hmg/7.5.839. PMID 9536088.
4. Chen, Y., Patel, N.A., Crombie, A., Scrivens, J.H. and Murrell, J.C. (2011). "Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase". Proc. Natl. Acad. Sci. USA 108 (43): 17791–17796. doi:10.1073/pnas.1112928108. PMC 3203794. PMID 22006322.

External links

• Trimethylamine monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)