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.^[1]

These enzymes metabolise xenobiotics^[2]. 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^{[3][4][5][6][7]}.

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.^[8] 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.^[9]

Genes

• FMO1, FMO2, FMO3, FMO4, FMO5

References

1. ^ Cashman JR (1995). "Structural and catalytic properties of the mammalian flavin-containing monooxygenase". Chem Res Toxicol 8 (2): 166–81. PMID 7766799. 
2. ^ 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. 
3. ^ 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. 
4. ^ 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. 
5. ^ 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. 
6. ^ 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. 
7. ^ 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. 
8. ^ 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. 
9. ^ 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. 

External links

• MeSH flavin-containing+monooxygenase
• EC 1.14.13.8

This protein-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Oxidoreductases Protein stubs Wikimedia Foundation. 2010. Игры ⚽ Нужна курсовая? Desolación Island Tipu Shah Look at other dictionaries: Flavin containing monooxygenase 3 — Flavin containing monooxygenase 3, also known as FMO3, is a human gene.cite web | title = Entrez Gene: FMO3 flavin containing monooxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=2328| accessdate …   Wikipedia Flavin containing monooxygenase 1 — Flavin containing monooxygenase 1, also known as FMO1, is a human gene.cite web | title = Entrez Gene: FMO1 flavin containing monooxygenase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=2326| accessdate …   Wikipedia Flavin-containing monooxygenase-3 (FMO3) — See Fish odor syndrome …   Medical dictionary Flavin containing amine oxidoreductase — Pfam box Symbol = Amino oxidase Name = Flavin containing amine oxidoreductase width = caption = Pfam= PF01593 InterPro= IPR002937 SMART= PROSITE = PDOC00755 SCOP = 1b37 TCDB = OPM family= 128 OPM protein= 1sez PDB=PDB3|1tdoA:61 499 PDB3|1tdkA:61… …   Wikipedia Methane monooxygenase — Particulate methane monooxygenase Identifiers Symbol pMMO Pfam PF02461 …   Wikipedia P450-containing systems — Any enzyme system that includes cytochrome P450 protein or domain can be called a P450 containing system. Contents 1 Overview 2 FR/Fd/P450 systems 3 CPR/P450 systems 4 CBR/b5/P450 systems …   Wikipedia FMO2 — Flavin containing monooxygenase 2 (non functional), also known as FMO2, is a human gene.cite web | title = Entrez Gene: FMO2 flavin containing monooxygenase 2 (non functional)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia FMO5 — Flavin containing monooxygenase 5, also known as FMO5, is a human gene. PBB Summary section title = summary text = Metabolic N oxidation of the diet derived amino trimethylamine (TMA) is mediated by flavin containing monooxygenase and is subject… …   Wikipedia FMO4 — Flavin containing monooxygenase 4, also known as FMO4, is a human gene.cite web | title = Entrez Gene: FMO4 flavin containing monooxygenase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=2329| accessdate …   Wikipedia Nitric oxide synthase — Identifiers EC number 1.14.13.39 CAS number 125978 95 2 …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”