- Flavin-containing monooxygenase
Flavin-containing monooxygenase FMO Identifiers Symbol Flavin_mOase Pfam PF00743 InterPro IPR000960 Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary
The flavin-containing monooxygenase (FMO) protein family consists of a group of enzymes that catalyze chemical reactions via the bound cofactor flavin. These reactions involve oxidation of heteroatoms, particularly nucleophilic atoms such as the nitrogen of amines.
These enzymes metabolise xenobiotics. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds. FMOs have been implicated in the metabolism of a number of pharmaceuticals, pesticides and toxicants. In man, lack of hepatic FMO-catalysed trimethylamine metabolism results in trimethylaminuria (fish odour syndrome). Five mammalian forms of FMO are now known and have been designated FMO1-FMO5.
The best-known such protein is called FMO3 and is mutated in the vast majority of cases of trimethylaminuria, a genetic disease that causes deficiencies in breakdown of trimethylamine and gives the patient a fishy body odor. In yeast, FMO proteins are associated with redox cycling of glutathione to glutathione disulfide, a system that maintains the redox state of the cell and heavily influences the protein folding rates of disulfide bond-containing proteins.
- ^ Cashman JR (1995). "Structural and catalytic properties of the mammalian flavin-containing monooxygenase". Chem Res Toxicol 8 (2): 166–81. PMID 7766799.
- ^ Lawton MP, Cashman JR, Cresteil T, Dolphin CT, Elfarra AA, Hines RN, Hodgson E, Kimura T, Ozols J, Phillips IR (1994). "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities". Arch. Biochem. Biophys. 308 (1): 254–257. doi:10.1006/abbi.1994.1035. PMID 8311461.
- ^ Phillips IR, Shephard EA, Ziegler DM, Povey S, Smith RL, Ayesh R, Dolphin C, Palmer CN (1991). "Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)". J. Biol. Chem. 266 (19): 12379–12385. PMID 1712018.
- ^ Lawton MP, Hodgson E, Philpot RM, Gasser R, Tynes RE (1990). "The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes". J. Biol. Chem. 265 (10): 5855–5861. PMID 2318837.
- ^ Cashman JR, Gu Q, Lomri N (1992). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1685–1689. doi:10.1073/pnas.89.5.1685. PMC 48517. PMID 1542660. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48517.
- ^ Dolphin CT, Phillips IR, Shephard EA, Povey S, Smith RL (1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". Biochem. J. 287: 261–267. PMC 1133153. PMID 1417778. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1133153.
- ^ Lawton MP, Philpot RM, Atta-Asafo-Adjei E (1993). "Cloning, sequencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1. Evidence for a third gene subfamily in rabbits". J. Biol. Chem. 268 (13): 9681–9689. PMID 8486656.
- ^ Hernandez D, Addou S, Lee D, Orengo C, Shephard EA, Phillips IR (September 2003). "Trimethylaminuria and a humanFMO3 mutation database". Human Mutation 22 (3): 209–13. doi:10.1002/humu.10252. PMID 12938085.
- ^ Suh JK, Poulsen LL, Ziegler DM, Robertus JD (1999). "Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum". Proc Natl Acad Sci 96 (6): 2687–91. doi:10.1073/pnas.96.6.2687. PMC 15830. PMID 10077572. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15830.
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) 1.14.11: 2-oxoglutarate 1.14.13: NADH or NADPH 1.14.14: reduced flavin or flavoprotein 1.14.15: reduced iron-sulfur protein 1.14.16: reduced pteridine (BH4 dependent) 1.14.17: reduced ascorbate 1.14.18-19: other 1.14.99 - miscellaneous This protein-related article is a stub. You can help Wikipedia by expanding it.