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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]
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.[2] 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.[3]
[edit] References
- ^ Cashman JR. (1995). Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem Res Toxicol 8(2):166-81. PMID 7766799
- ^ Hernandez D, Addou S, Lee D, Orengo C, Shephard EA, Phillips IR (2003). Trimethylaminuria and a human FMO3 mutation database. Hum Mutat 22 (3): 209-13. 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. PMID 10077572
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