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Flavin containing monooxygenase 2 (non-functional)
Symbols FMO2 ; FMO 1B1; FMO 2; FMO1B1
External IDs OMIM603955 MGI1916776 HomoloGene86882 GeneCards: FMO2 Gene
EC number
RNA expression pattern
PBB GE FMO2 211726 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2327 55990
Ensembl ENSG00000094963 ENSMUSG00000040170
UniProt Q99518 Q8K2I3
RefSeq (mRNA) NM_001460 NM_018881
RefSeq (protein) NP_001451 NP_061369
Location (UCSC) Chr 1:
171.15 – 171.18 Mb
Chr 1:
162.87 – 162.9 Mb
PubMed search [1] [2]

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]


  1. ^ 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): 261–7. PMC 1133153. PMID 1417778. 
  2. ^ 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. 
  3. ^ a b "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)". 

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