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Gene Review

Fmo5  -  flavin containing monooxygenase 5

Mus musculus

Synonyms: 5033418D19Rik, AI195026, Dimethylaniline oxidase 5, FMO 5, Hepatic flavin-containing monooxygenase 5
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Disease relevance of Fmo5


High impact information on Fmo5

  • OBJECTIVES: To date, six flavin-containing monooxygenase (FMO) genes have been identified in humans, FMOs 1, 2, 3, 4 and 6, which are located within a cluster on chromosome 1, and FMO5, which is located outside the cluster [2].
  • RNase protection assays showed that the most abundant isoform in newborn liver, lung, kidney and brain, and in adult lung and kidney is FMO1, but in adult liver FMO5 is present in greatest amounts [3].
  • The Km value for tamoxifen is 1.2 mM for mouse FMO1 (human FMO1 is not expressed in adults) and 1.4 mM for human FMO3, with no detectable activity being expressed toward tamoxifen by FMO5 from either mouse or human [4].
  • In addition, FMO1 was shown to metabolize radiolabeled phorate, whereas FMO5 showed no activity toward phorate [1].
  • Molecular cloning, sequence, and expression of mouse flavin-containing monooxygenases 1 and 5 (FMO1 and FMO5) [1].

Associations of Fmo5 with chemical compounds

  • Two GxGxxG putative pyrophosphate binding domains exist beginning at positions 9 and 191 for FMO1, and 10 and 192 for FMO5 [1].
  • The expressed FMO1 protein showed activity toward methimazole, and FMO5 was active toward noctylamine [1].


  1. Molecular cloning, sequence, and expression of mouse flavin-containing monooxygenases 1 and 5 (FMO1 and FMO5). Cherrington, N.J., Falls, J.G., Rose, R.L., Clements, K.M., Philpot, R.M., Levi, P.E., Hodgson, E. J. Biochem. Mol. Toxicol. (1998) [Pubmed]
  2. Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: identification of novel gene and pseudogene clusters. Hernandez, D., Janmohamed, A., Chandan, P., Phillips, I.R., Shephard, E.A. Pharmacogenetics (2004) [Pubmed]
  3. Cell-, tissue-, sex- and developmental stage-specific expression of mouse flavin-containing monooxygenases (Fmos). Janmohamed, A., Hernandez, D., Phillips, I.R., Shephard, E.A. Biochem. Pharmacol. (2004) [Pubmed]
  4. Flavin-containing monooxygenase isoform specificity for the N-oxidation of tamoxifen determined by product measurement and NADPH oxidation. Hodgson, E., Rose, R.L., Cao, Y., Dehal, S.S., Kupfer, D. J. Biochem. Mol. Toxicol. (2000) [Pubmed]
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