Description
Product Characteristics:
The Flavin containing monooxygenase family consists of five gene products, FMO1-5, that are major enzymatic oxidants involved in the metabolism of various therapeutics. Located in the liver, FMO3 is a hepatic microsomal enzyme that oxygenates soft nucleophiles such as secondary and tertiary amines. Through its N-oxygenase capabilities, FMO3 acts on a variety of xenobiotics to catalyze oxidative digestion. Defects in the FMO3 gene are the primary cause of trimethylaminuria (TMAuria), an inborn error of metabolism associated with a fishy body odor emitting from sweat, urine and breath. Genetic mutations in FMO3 lead to the N-oxidation of amino-trimethylamine derived from food products, thus producing the malodor associated with TMAuria.
Subcellular location: Cytoplasm, Cell membrane
Synonyms: Dimethylaniline monooxygenase [N oxide forming] 3, Dimethylaniline monooxygenase [N-oxide-forming] 3, Dimethylaniline monooxygenase 3, Dimethylaniline oxidase 3, dJ127D3.1, Flavin containing monooxygenase 3, FMO 3, FMO form 2, FMO II, FMO3, FMO3_HUMAN, FMOII, Hepatic flavin containing monooxygenase 3, Hepatic flavin-containing monooxygenase 3, MGC34400, TMAU, Trimethylamine monooxygenase.
Target Information: Flavin-containing monooxygenases (FMO) are an important class of drug-metabolizing enzymes that catalyze the NADPH-dependent oxygenation of various nitrogen-,sulfur-, and phosphorous-containing xenobiotics such as therapeutic drugs, dietary compounds, pesticides, and other foreign compounds. The human FMO gene family is composed of 5 genes and multiple pseudogenes. FMO members have distinct developmental- and tissue-specific expression patterns. The expression of this FMO3 gene, the major FMO expressed in adult liver, can vary up to 20-fold between individuals. This inter-individual variation in FMO3 expression levels is likely to have significant effects on the rate at which xenobiotics are metabolised and, therefore, is of considerable interest to the pharmaceutical industry. This transmembrane protein localizes to the endoplasmic reticulum of many tissues. Alternative splicing of this gene results in multiple transcript variants encoding the same protein. Mutations in this gene cause the disorder trimethylaminuria (TMAu) which is characterized by the accumulation and excretion of unmetabolized trimethylamine and a distinctive body odor. In healthy individuals, trimethylamine is primarily converted to the non odorous trimethylamine N-oxide.[provided by RefSeq, Aug 2009]