From Wikipedia, the free encyclopedia
Jump to: navigation, search
Flavin containing monooxygenase 5
Symbol FMO5
External IDs OMIM603957 MGI1310004 HomoloGene68185 GeneCards: FMO5 Gene
EC number
RNA expression pattern
PBB GE FMO5 205776 at tn.png
PBB GE FMO5 215300 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2330 14263
Ensembl ENSG00000131781 ENSMUSG00000028088
UniProt P49326 P97872
RefSeq (mRNA) NM_001144829 NM_001161763
RefSeq (protein) NP_001138301 NP_001155235
Location (UCSC) Chr 1:
147.18 – 147.24 Mb
Chr 3:
97.63 – 97.66 Mb
PubMed search [1] [2]

Dimethylaniline monooxygenase [N-oxide-forming] 5 is an enzyme that in humans is encoded by the FMO5 gene.[1][2][3]

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 man 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 drugs, pesticides, and xenobiotics.[3]

Related gene problems[edit]


  1. ^ McCombie RR, Dolphin CT, Povey S, Phillips IR, Shephard EA (Sep 1996). "Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q". Genomics 34 (3): 426–9. doi:10.1006/geno.1996.0308. PMID 8786146. 
  2. ^ Gelb BD, Zhang J, Cotter PD, Gershin IF, Desnick RJ (Apr 1997). "Physical mapping of the human connexin 40 (GJA5), flavin-containing monooxygenase 5, and natriuretic peptide receptor a genes on 1q21". Genomics 39 (3): 409–11. doi:10.1006/geno.1996.4516. PMID 9119381. 
  3. ^ a b "Entrez Gene: FMO5 flavin containing monooxygenase 5". 

Further reading[edit]

  • 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. 
  • 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. 
  • Overby LH, Buckpitt AR, Lawton MP et al. (1995). "Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog.". Arch. Biochem. Biophys. 317 (1): 275–84. doi:10.1006/abbi.1995.1163. PMID 7872795. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • 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): 254–7. doi:10.1006/abbi.1994.1035. PMID 8311461. 
  • Overby LH, Carver GC, Philpot RM (1997). "Quantitation and kinetic properties of hepatic microsomal and recombinant flavin-containing monooxygenases 3 and 5 from humans". Chem. Biol. Interact. 106 (1): 29–45. doi:10.1016/S0009-2797(97)00055-0. PMID 9305407. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Chung WG, Park CS, Roh HK et al. (2001). "Oxidation of ranitidine by isozymes of flavin-containing monooxygenase and cytochrome P450". Jpn. J. Pharmacol. 84 (2): 213–20. doi:10.1254/jjp.84.213. PMID 11128045. 
  • Janmohamed A, Dolphin CT, Phillips IR, Shephard EA (2001). "Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450". Biochem. Pharmacol. 62 (6): 777–86. doi:10.1016/S0006-2952(01)00718-3. PMID 11551524. 
  • 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): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Krause RJ, Lash LH, Elfarra AA (2003). "Human kidney flavin-containing monooxygenases and their potential roles in cysteine s-conjugate metabolism and nephrotoxicity". J. Pharmacol. Exp. Ther. 304 (1): 185–91. doi:10.1124/jpet.102.042911. PMID 12490590. 
  • 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): 187–93. doi:10.1124/dmd.31.2.187. PMID 12527699. 
  • Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • 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. 
  • Gregory SG, Barlow KF, McLay KE et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.