Flavin containing monooxygenase 1

Flavin containing monooxygenase 1
Identifiers
Symbol	FMO1
External IDs	OMIM: 136130 MGI: 1310002 HomoloGene: 55520 GeneCards: FMO1 Gene
EC number	1.14.13.8
Gene ontology Molecular function • monooxygenase activity • N,N-dimethylaniline monooxygenase activity • flavin adenine dinucleotide binding • NADP binding Cellular component • endoplasmic reticulum lumen • endoplasmic reticulum membrane • integral component of membrane Biological process • organic acid metabolic process • xenobiotic metabolic process • response to osmotic stress • toxin metabolic process • drug metabolic process • response to lipopolysaccharide • small molecule metabolic process • NADPH oxidation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2326	14261
Ensembl	ENSG00000010932	ENSMUSG00000040181
UniProt	Q01740	P50285
RefSeq (mRNA)	NM_001282692	NM_010231
RefSeq (protein)	NP_001269621	NP_034361
Location (UCSC)	Chr 1: 171.25 – 171.29 Mb	Chr 1: 162.83 – 162.87 Mb
PubMed search

Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene.^[1]

Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in humans resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in xenobiotics such as pesticides and drugs.^[1]

References

1. "Entrez Gene: FMO1 flavin containing monooxygenase 1".

Further reading

• Hines RN, Cashman JR, Philpot RM, et al. (1994). "The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression". Toxicol. Appl. Pharmacol. 125 (1): 1–6. doi:10.1006/taap.1994.1042. PMID 8128486.
• Cashman JR (2004). "The implications of polymorphisms in mammalian flavin-containing monooxygenases in drug discovery and development". Drug Discov. Today 9 (13): 574–581. doi:10.1016/S1359-6446(04)03136-8. PMID 15203093.
• Dolphin C, Shephard EA, Povey S, et al. (1991). "Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)". J. Biol. Chem. 266 (19): 12379–85. PMID 1712018.
• Phillips IR, Dolphin CT, Clair P, et al. (1995). "The molecular biology of the flavin-containing monooxygenases of man". Chem. Biol. Interact. 96 (1): 17–32. doi:10.1016/0009-2797(94)03580-2. PMID 7720101.
• Lawton MP, Cashman JR, Cresteil T, et al. (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. PMID 8311461.
• Shephard EA, Dolphin CT, Fox MF, et al. (1993). "Localization of genes encoding three distinct flavin-containing monooxygenases to human chromosome 1q". Genomics 16 (1): 85–89. doi:10.1006/geno.1993.1144. PMID 8486388.
• Hay JC, Chao DS, Kuo CS, Scheller RH (1997). "Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells". Cell 89 (1): 149–158. doi:10.1016/S0092-8674(00)80191-9. PMID 9094723.
• Yeung CK, Lang DH, Thummel KE, Rettie AE (2000). "Immunoquantitation of FMO1 in human liver, kidney, and intestine". Drug Metab. Dispos. 28 (9): 1107–11. PMID 10950857.
• Washio T, Arisawa H, Kohsaka K, Yasuda H (2002). "Identification of human drug-metabolizing enzymes involved in the metabolism of SNI-2011". Biol. Pharm. Bull. 24 (11): 1263–1266. doi:10.1248/bpb.24.1263. PMID 11725960.
• Koukouritaki SB, Simpson P, Yeung CK, et al. (2002). "Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression". Pediatr. Res. 51 (2): 236–243. doi:10.1203/00006450-200202000-00018. PMID 11809920.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Furnes B, Feng J, Sommer SS, Schlenk D (2003). "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans". Drug Metab. Dispos. 31 (2): 187–193. doi:10.1124/dmd.31.2.187. PMID 12527699.
• Attar M, Dong D, Ling KH, Tang-Liu DD (2003). "Cytochrome P450 2C8 and flavin-containing monooxygenases are involved in the metabolism of tazarotenic acid in humans". Drug Metab. Dispos. 31 (4): 476–481. doi:10.1124/dmd.31.4.476. PMID 12642475.
• Hines RN, Luo Z, Hopp KA, et al. (2003). "Genetic variability at the human FMO1 locus: significance of a basal promoter yin yang 1 element polymorphism (FMO1*6)". J. Pharmacol. Exp. Ther. 306 (3): 1210–1218. doi:10.1124/jpet.103.053686. PMID 12829732.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Zhang J, Cashman JR (2006). "Quantitative analysis of FMO gene mRNA levels in human tissues". Drug Metab. Dispos. 34 (1): 19–26. doi:10.1124/dmd.105.006171. PMID 16183778.
• Bartsch M, Gobbato E, Bednarek P, et al. (2006). "Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1 and the Nudix hydrolase NUDT7". Plant Cell 18 (4): 1038–1051. doi:10.1105/tpc.105.039982. PMC 1425861. PMID 16531493.