Flavin monooxygenase FMO
IPR000960
Definition
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes PMID:8311461. 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 [[cite:PMID:1712018], [cite:PMID:2318837], [cite:PMID:1542660], [cite:PMID:1417778], [cite:PMID:8486656], [cite:PMID:32156684]]. This is a recent nomenclature based on comparison of amino acid sequences, and has been introduced in an attempt to eliminate confusion inherent in multiple, laboratory-specific designations and tissue-based classifications PMID:8311461. Following the determination of the complete nucleotide sequence of Saccharomyces cerevisiae (Baker's yeast) PMID:8091229, a novel gene was found to encode a protein with similarity to mammalian monooxygenases. In Aspergillus, flavin-containing monooxygenases ustF1 and ustF2 are components in the biosynthesis of the antimitotic tetrapeptide ustiloxin B, a secondary metabolite. The monooxygenases modify the side chain of the intermediate S-deoxyustiloxin H PMID:27166860.
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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