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Flavin-containing monooxygenase 3

Protein-coding gene in the species Homo sapiens

Protein-coding gene in the species Homo sapiens

Flavin-containing monooxygenase 3 (FMO3), also known as dimethylaniline monooxygenase [N-oxide-forming] 3 and trimethylamine monooxygenase, is a flavoprotein enzyme () that in humans is encoded by the FMO3 gene. This enzyme catalyzes the following chemical reaction, among others:

:trimethylamine + NADPH + H+ + O2 \rightleftharpoons trimethylamine N-oxide + NADP+ + H2O

FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. The human FMO3 enzyme catalyzes several types of reactions, including: the N-oxygenation of primary, secondary, and tertiary amines; the S-oxygenation of nucleophilic sulfur-containing compounds; and the 6-methylhydroxylation of the anti-cancer agent dimethylxanthenone acetic acid (DMXAA).

FMO3 is the primary enzyme in humans which catalyzes the N-oxidation of trimethylamine into trimethylamine N-oxide; FMO1 also does this, but to a much lesser extent than FMO3. Genetic deficiencies of the FMO3 enzyme cause primary trimethylaminuria, also known as "fish odor syndrome". FMO3 is also involved in the metabolism of many xenobiotics (i.e., exogenous compounds which are not normally present in the body), such as the oxidative deamination of amphetamine.

Ligands

FMO3 substratesFMO3 inhibitorsFMO3 inducersFMO3 activatorsA † indicates moderate to complete selectivity for FMO3 relative to other FMO isoenzymes.

Cancer

The FMO3 gene has been observed progressively downregulated in human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, FMO3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for progression of uterine cervical preneoplastic lesions.

References

References

  1. (June 1993). "Localization of genes encoding three distinct flavin-containing monooxygenases to human chromosome 1q". Genomics.
  2. (February 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.
  3. "Entrez Gene: FMO3 flavin containing monooxygenase 3".
  4. (July 2002). "6-methylhydroxylation of the anti-cancer agent 5,6-dimethylxanthenone-4-acetic acid (DMXAA) by flavin-containing monooxygenase 3". Eur J Drug Metab Pharmacokinet.
  5. (October 2014). "The contributory role of gut microbiota in cardiovascular disease". J. Clin. Invest..
  6. (2013). "Trimethylamine-N-oxide, a metabolite associated with atherosclerosis, exhibits complex genetic and dietary regulation". Cell Metab..
  7. (1997). "Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome". Nat. Genet..
  8. (June 2005). "Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism". Pharmacol. Ther..
  9. Glennon RA. (2013). "Foye's principles of medicinal chemistry". Wolters Kluwer Health/Lippincott Williams & Wilkins.
  10. (March 1999). "N-oxygenation of amphetamine and methamphetamine by the human flavin-containing monooxygenase (form 3): role in bioactivation and detoxication". J. Pharmacol. Exp. Ther..
  11. (August 2016). "Association of FMO3 Variants and Trimethylamine N-Oxide Concentration, Disease Progression, and Mortality in CKD Patients". PLOS ONE.
  12. (June 2007). "Genetic polymorphisms of human flavin-containing monooxygenase 3: implications for drug metabolism and clinical perspectives". Pharmacogenomics.
  13. (September 2000). "Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism". Curr. Drug Metab..
  14. (July 2016). "Trimethylamine monooxygenase (Homo sapiens) {{!}} BRENDA". Technische Universität Braunschweig.
  15. (September 1999). "In vitro and in vivo inhibition of human flavin-containing monooxygenase form 3 (FMO3) in the presence of dietary indoles". Biochemical Pharmacology.
  16. (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes.". J Cell Physiol.
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