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Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.[5][6][7]

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.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000094963Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040170Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (Nov 1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". Biochem J. 287. ( Pt 1) (Pt 1): 261–7. doi:10.1042/bj2870261. PMC 1133153. PMID 1417778.
  6. ^ Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR (Dec 1998). "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. doi:10.1074/jbc.273.46.30599. PMID 9804831.
  7. ^ a b "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)".

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