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Gene Review

FMO1  -  flavin containing monooxygenase 1

Canis lupus familiaris

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High impact information on FMO1

  • The amino acid sequence of dFMO1 was 89% homologous to human FMO1 [1].
  • By Western blotting, dog FMO1 and dog FMO3 were detected in microsomes from liver and lung but not in kidney microsomes [2].
  • The cDNAs of dog FMO1 and dog FMO3 encode proteins of 532 amino acids, which contain the NADPH- and FAD-binding sites [2].
  • Methionine has previously been shown to be S-oxidized by flavin-containing monooxygenase (FMO) forms 1, 2, and 3 [3].
  • 4. Human flavin-containing monooxygenase form 3 (FMO3) catalysed exclusively the N-oxidation to M3, with apparent Km and optimum pH comparable with those observed in human liver microsomes [4].

Biological context of FMO1

  • The use of enzyme inhibitors, activators and inducers indicated that EMA N-oxide formation was predominantly mediated by FMO in the presence of rabbit hepatic microsomes and that these agents did not generally affect the stereochemical outcome of the biotransformation [5].

Anatomical context of FMO1


Analytical, diagnostic and therapeutic context of FMO1

  • By Northern blotting, the probe for FMO1 specifically hybridized a 2.6-kilobase (kb) transcript in liver and lung samples only [2].


  1. Expression and characterization of functional dog flavin-containing monooxygenase 1. Stevens, J.C., Melton, R.J., Zaya, M.J., Engel, L.C. Mol. Pharmacol. (2003) [Pubmed]
  2. Cloning, sequencing, and tissue-dependent expression of flavin-containing monooxygenase (FMO) 1 and FMO3 in the dog. Lattard, V., Longin-Sauvageon, C., Lachuer, J., Delatour, P., Benoit, E. Drug Metab. Dispos. (2002) [Pubmed]
  3. Methionine S-oxidation in human and rabbit liver microsomes: evidence for a high-affinity methionine S-oxidase activity that is distinct from flavin-containing monooxygenase 3. Ripp, S.L., Itagaki, K., Philpot, R.M., Elfarra, A.A. Arch. Biochem. Biophys. (1999) [Pubmed]
  4. Interspecies comparison and role of human cytochrome P450 and flavin-containing monooxygenase in hepatic metabolism of L-775,606, a potent 5-HT(1D) receptor agonist. Prueksaritanont, T., Lu, P., Gorham, L., Sternfeld, F., Vyas, K.P. Xenobiotica (2000) [Pubmed]
  5. Species differences in the stereoselectivity of N-oxygenation of N-ethyl-N-methylaniline in vitro. Hadley, M.R., Oldham, H.G., Camilleri, P., Damani, L.A., Hutt, A.J. Chirality. (1996) [Pubmed]
  6. Estimation of flavin-containing monooxygenase activity in intact hepatocyte monolayers of rat, hamster, rabbit, dog and human by using N-oxidation of benzydamine. Ubeaud, G., Schiller, C.D., Hurbin, F., Jaeck, D., Coassolo, P. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. (1999) [Pubmed]
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