Flavin_containing_monooxygenase_1

FMO1
Identifiers
Aliases	FMO1, flavin containing monooxygenase 1, flavin containing dimethylaniline monoxygenase 1
External IDs	OMIM: 136130 MGI: 1310002 HomoloGene: 55520 GeneCards: FMO1
Gene location (Human)
Chr.	Chromosome 1 (human)
End	171,285,978 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	162,694,179 bp
RNA expression pattern
	Top expressed in
	kidney tubule; ; glomerulus; ; kidney; ; metanephric glomerulus; ; parietal pleura; ; renal medulla; ; cavity of mouth; ; gallbladder; ; lactiferous duct; ; left uterine tube;
	Top expressed in
	kidney; ; yolk sac; ; proximal tubule; ; right lung; ; brown adipose tissue; ; right lung lobe; ; left lobe of liver; ; intercostal muscle; ; white adipose tissue; ; carotid body;
	More reference expression data
	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
	2326
	14261
	ENSG00000010932
	ENSMUSG00000040181
	Q01740
	P50285
	NM_001282692; NM_001282693; NM_001282694; NM_002021
	NM_010231; NM_001330291; NM_001330318
	NP_001269621; NP_001269622; NP_001269623; NP_002012
	NP_001317220; NP_001317247; NP_034361
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000010932 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000040181 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: FMO1 flavin containing monooxygenase 1".

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. doi:10.1016/S0021-9258(18)98908-8. 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. 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, 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. 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, 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. S2CID 25093628.
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. S2CID 1784074.
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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000010932 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-5] "Entrez Gene: FMO1 flavin containing monooxygenase 1".

[1]

[2]

[3]

[4]

[5]

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

Flavin_containing_monooxygenase_1

References

Further reading