Flavin containing monooxygenase 1

Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene.^[5]

FMO1
Identifiers
Aliases	FMO1, flavin containing monooxygenase 1, flavin containing dimethylaniline monoxygenase 1
External IDs	OMIM: 136130; MGI: 1310002; HomoloGene: 55520; GeneCards: FMO1; OMA:FMO1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q24.3 Start 171,248,471 bp[1] End 171,285,978 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 H2.1|1 70.34 cM Start 162,657,130 bp[2] End 162,694,179 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in kidney tubule glomerulus metanephric glomerulus human kidney mucosa of ileum parietal pleura mucosa of paranasal sinus renal medulla oral cavity skin of thigh Top expressed in right kidney human kidney yolk sac gastrula proximal tubule right lung tunica adventitia of aorta brown adipose tissue right lung lobe cardiac muscle tissue of left ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function oxidoreductase activity N,N-dimethylaniline monooxygenase activity NADP binding flavin adenine dinucleotide binding monooxygenase activity protein binding Cellular component organelle membrane integral component of membrane endoplasmic reticulum lumen endoplasmic reticulum membrane endoplasmic reticulum membrane intracellular membrane-bounded organelle Biological process response to osmotic stress xenobiotic metabolic process toxin metabolic process response to lipopolysaccharide NADPH oxidation organic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2326 14261 Ensembl ENSG00000010932 ENSMUSG00000040181 UniProt Q01740 P50285 RefSeq (mRNA) NM_001282692 NM_001282693 NM_001282694 NM_002021 NM_010231 NM_001330291 NM_001330318 RefSeq (protein) NP_001269621 NP_001269622 NP_001269623 NP_002012 NP_001317220 NP_001317247 NP_034361 Location (UCSC) Chr 1: 171.25 – 171.29 Mb Chr 1: 162.66 – 162.69 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000010932 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040181 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: FMO1 flavin containing monooxygenase 1".

Further reading

• Hines RN, Cashman JR, Philpot RM, Williams DE, Ziegler DM (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, Palmer CN, Ziegler DM, Ayesh R, et al. (1991). "Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)". J. Biol. Chem. 266 (19): 12379–85. doi:10.1016/S0021-9258(18)98908-8. PMID 1712018.
• Phillips IR, Dolphin CT, Clair P, Hadley MR, Hutt AJ, McCombie RR, et al. (1995). "The molecular biology of the flavin-containing monooxygenases of man". Chem. Biol. Interact. 96 (1): 17–32. Bibcode:1995CBI....96...17P. doi:10.1016/0009-2797(94)03580-2. PMID 7720101.
• Lawton MP, Cashman JR, Cresteil T, Dolphin CT, Elfarra AA, Hines RN, 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, Povey S, Smith R, Phillips IR (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. S2CID 8682509.
• 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, Rettie AE, Hines RN (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, Derge JG, Klausner RD, Collins FS, 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. Bibcode:2002PNAS...9916899M. 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. S2CID 6619389.
• 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, Cabacungan ET, Koukouritaki SB, McCarver DG (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. S2CID 25093628.
• Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, 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, Shenmen CM, Grouse LH, Schuler G, 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. S2CID 1784074.
• Bartsch M, Gobbato E, Bednarek P, Debey S, Schultze JL, Bautor J, 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.