Flavin containing monooxygenase 3

From Wikipedia, the free encyclopedia

Identifiers

FMO3; FMOII; MGC34400; dJ127D3.1

External IDs

OMIM: 136132 MGI: 1100496 HomoloGene: 68130

Gene ontology
Molecular Function:	• monooxygenase activity • flavin-containing monooxygenase activity • disulfide oxidoreductase activity • FAD binding • NADP binding
Cellular Component:	• endoplasmic reticulum • microsome • membrane • integral to membrane • intrinsic to endoplasmic reticulum membrane
Biological Process:	• electron transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001002294 (mRNA)
NP_001002294 (protein)

NM_008030 (mRNA)
NP_032056 (protein)

Location

Chr 1: 169.33 - 169.35 Mb

Chr 1: 164.79 - 164.82 Mb

Pubmed search

[1]

[2]

Flavin containing monooxygenase 3, also known as FMO3, is a human gene.^[1]

[edit] See also

Flavin-containing monooxygenase

[edit] References

^ Entrez Gene: FMO3 flavin containing monooxygenase 3.

[edit] Further reading

Cashman JR, Park SB, Berkman CE, Cashman LE (1995). "Role of hepatic flavin-containing monooxygenase 3 in drug and chemical metabolism in adult humans.". Chem. Biol. Interact. 96 (1): 33–46. PMID 7720103.
Cashman JR (2004). "The implications of polymorphisms in mammalian flavin-containing monooxygenases in drug discovery and development.". Drug Discov. Today 9 (13): 574–81. doi:10.1016/S1359-6446(04)03136-8. PMID 15203093.
Zhou J, Shephard EA (2006). "Mutation, polymorphism and perspectives for the future of human flavin-containing monooxygenase 3.". Mutat. Res. 612 (3): 165–71. doi:10.1016/j.mrrev.2005.09.001. PMID 16481213.
Lomri N, Gu Q, Cashman JR (1992). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1685–9. PMID 1542660.
Humbert JA, Hammond KB, Hathaway WE (1970). "Trimethylaminuria: the fish-odour syndrome.". Lancet 2 (7676): 770–1. PMID 4195988.
Higgins T, Chaykin S, Hammond KB, Humbert JR (1972). "Trimethylamine N-oxide synthesis: a human variant.". Biochemical medicine 6 (4): 392–6. PMID 5048998.
Lomri N, Gu Q, Cashman JR (1995). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.". Proc. Natl. Acad. Sci. U.S.A. 92 (21): 9910. PMID 7568243.
Bhamre S, Bhagwat SV, Shankar SK, et al. (1995). "Flavin-containing monooxygenase mediated metabolism of psychoactive drugs by human brain microsomes.". Brain Res. 672 (1-2): 276–80. PMID 7749747.
Cashman JR, Park SB, Yang ZC, et al. (1993). "Chemical, enzymatic, and human enantioselective S-oxygenation of cimetidine.". Drug Metab. Dispos. 21 (4): 587–97. PMID 8104117.
Park SB, Jacob P, Benowitz NL, Cashman JR (1994). "Stereoselective metabolism of (S)-(-)-nicotine in humans: formation of trans-(S)-(-)-nicotine N-1'-oxide.". Chem. Res. Toxicol. 6 (6): 880–8. PMID 8117928.
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. PMID 8125298.
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): 85–9. doi:10.1006/geno.1993.1144. PMID 8486388.
Dolphin CT, Cullingford TE, Shephard EA, et al. (1996). "Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04.". Eur. J. Biochem. 235 (3): 683–9. PMID 8654418.
Chung WG, Cha YN (1997). "Oxidation of caffeine to theobromine and theophylline is catalyzed primarily by flavin-containing monooxygenase in liver microsomes.". Biochem. Biophys. Res. Commun. 235 (3): 685–8. doi:10.1006/bbrc.1997.6866. PMID 9207220.
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. PMID 9373149.
Dolphin CT, Janmohamed A, Smith RL, et al. (1997). "Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome.". Nat. Genet. 17 (4): 491–4. doi:10.1038/ng1297-491. PMID 9398858.
Dolphin CT, Riley JH, Smith RL, et al. (1998). "Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA.". Genomics 46 (2): 260–7. doi:10.1006/geno.1997.5031. PMID 9417913.
Treacy EP, Akerman BR, Chow LM, et al. (1998). "Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication.". Hum. Mol. Genet. 7 (5): 839–45. PMID 9536088.
Akerman BR, Forrest S, Chow L, et al. (1999). "Two novel mutations of the FMO3 gene in a proband with trimethylaminuria.". Hum. Mutat. 13 (5): 376–9. doi:10.1002/(SICI)1098-1004(1999)13:5<376::AID-HUMU5>3.0.CO;2-A. PMID 10338091.