These enzymes metabolise xenobiotics. 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 humans, 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.
^Cashman JR (1995). "Structural and catalytic properties of the mammalian flavin-containing monooxygenase". Chem Res Toxicol8 (2): 166–81. doi:10.1021/tx00044a001. PMID7766799.
^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. PMID8311461.
^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. PMID1712018.
^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. PMID2318837.
^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. PMID8486656.
^Hernandez D, Addou S, Lee D, Orengo C, Shephard EA, Phillips IR (September 2003). "Trimethylaminuria and a humanFMO3 mutation database". Human Mutation22 (3): 209–13. doi:10.1002/humu.10252. PMID12938085.