Flavin monooxygenase (FMO) 5
InterPro Protein Domain record
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description
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Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [<cite idref="PUB00000158"/>]. Using an NADPH cofactor and FAD prosthetic group,these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen,sulphur, phosphorous and selenium atoms in a range of structurally diversecompounds. Five mammalian forms of FMO are now known and have been designatedFMO1-FMO5 [<cite idref="PUB00002642"/>, <cite idref="PUB00002611"/>, <cite idref="PUB00004772"/>, <cite idref="PUB00000516"/>, <cite idref="PUB00002834"/>].<p>The deduced amino acid sequence of human FM05 includes the putative FAD- (GxGxxG) and NADP<sup>+</sup> pyrophosphate-binding (GxGxxA) sites characteristic of mammalian FMOs [<cite idref="PUB00002364"/>], a 'FATGY' motif that has also been observed in a rangeof siderphore biosynthetic enzymes [<cite idref="PUB00005489"/>], and a C-terminal hydrophobic segmentthat is believed to anchor the monooxygenase to the microsomal membrane [<cite idref="PUB00002549"/>].Human and guinea pig FMO5, like other FMOs, are encoded by multipletranscripts. FMO5 has been identified in livers of adult humans, rabbitsand guinea pigs, and foetal livers of humans [<cite idref="PUB00000162"/>]. Neither the human nor guinea pig enzyme effectively catalyse the metabolism of methimazole, ageneral FMO substrate; however, both are active with n-octylamine [<cite idref="PUB00000162"/>]. Theresponses to detergent, ions and elevated temperature are all similar to those observed in rabbit FMO5, suggesting that these properties are species-independent and that this form of FMO is not readily classified as a drug-metabolising enzyme [<cite idref="PUB00000162"/>].</p>
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Flavin monooxygenase (FMO) 5
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InterPro Protein Domain record
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