Biology:FMO2

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.[1][2][3]

The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.[3]

References

  1. "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". Biochem J. 287 ( Pt 1): 261–7. Nov 1992. doi:10.1042/bj2870261. PMID 1417778. 
  2. "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein". J Biol Chem 273 (46): 30599–607. Dec 1998. doi:10.1074/jbc.273.46.30599. PMID 9804831. 
  3. 3.0 3.1 "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2327. 

Further reading