Flavin containing monooxygenase 3

Identifiers

FMO3; FMOII; MGC34400; TMAU; dJ127D3.1

External IDs

OMIM: 136132 MGI: 1100496 HomoloGene: 68130 GeneCards: FMO3 Gene

1.14.13.8

Gene Ontology
Molecular function	• monooxygenase activity • flavin-containing monooxygenase activity • amino acid binding • flavin adenine dinucleotide binding • NADP binding
Cellular component	• endoplasmic reticulum • endoplasmic reticulum membrane • microsome • membrane • integral to membrane • intrinsic to endoplasmic reticulum membrane
Biological process	• xenobiotic metabolic process • drug metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
171.06 – 171.09 Mb

Chr 1:
164.88 – 164.91 Mb

PubMed search

[1]

[2]

Dimethylaniline monooxygenase [N-oxide-forming] 3 is an enzyme that in humans is encoded by the FMO3 gene.^[1]^[2]^[3]

1 External Links
2 See also
3 References
4 Further reading

External Links

GeneReviews/NCBI/NIH/UW entry on Trimethylaminuria or Fish Odor Syndrome

References

^ Shephard EA, Dolphin CT, Fox MF, Povey S, Smith R, Phillips IR (Jun 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, Riley JH, Smith RL, Shephard EA, Phillips IR (Feb 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.
^ "Entrez Gene: FMO3 flavin containing monooxygenase 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2328.

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. doi:10.1016/0009-2797(94)03581-R. 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. doi:10.1073/pnas.89.5.1685. PMC 48517. PMID 1542660. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48517.
Humbert JA, Hammond KB, Hathaway WE (1970). "Trimethylaminuria: the fish-odour syndrome.". Lancet 2 (7676): 770–1. doi:10.1016/S0140-6736(70)90241-2. PMID 4195988.
Higgins T, Chaykin S, Hammond KB, Humbert JR (1972). "Trimethylamine N-oxide synthesis: a human variant.". Biochemical medicine 6 (4): 392–6. doi:10.1016/0006-2944(72)90025-7. 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. doi:10.1073/pnas.92.21.9910. PMC 40912. PMID 7568243. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40912.
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. doi:10.1016/0006-8993(94)01135-5. 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. doi:10.1021/tx00036a019. 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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. doi:10.1111/j.1432-1033.1996.00683.x. 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. doi:10.1016/S0378-1119(97)00411-3. 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.
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. doi:10.1093/hmg/7.5.839. 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.

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase - Lysyl hydroxylase

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 - Lanosterol 14 alpha-demethylase

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

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Transferase: nitrogenous groups (EC 2.6)

2.6.1: Transaminases	Aspartate transaminase (GOT1, GOT2) · Alanine transaminase · GABA transaminase · Tyrosine aminotransferase · Ornithine aminotransferase · Branched chain aminotransferase · Alanine-glyoxylate transaminase (AGXT)

2.6.3: Oximinotransferases	Oximinotransferase

2.6.99: Other	Pyridoxine 5'-phosphate synthase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Flavin containing monooxygenase 3

Contents

External Links

See also

References

Further reading