The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

FMO5  -  flavin containing monooxygenase 5

Homo sapiens

Synonyms: Dimethylaniline oxidase 5, FMO 5, Hepatic flavin-containing monooxygenase 5
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of FMO5


High impact information on FMO5


Biological context of FMO5


Anatomical context of FMO5

  • In contrast, an immortalized human keratinocyte cell line, HaCaT, expressed FMO3, FMO5, and CYP2B6 mRNAs in amounts that fall within the range detected in the whole skin samples analysed [7].
  • 4. The apparent K(m) (K(m app)) for the S-oxidation of M2 in human recombinant FMO5 (2.71 microM) was similar to that obtained using human liver microsomes (2.43 microM) [8].

Associations of FMO5 with chemical compounds

  • FMO2 and FMO5, although expressed slightly in human liver, kidney and lung, were not efficient producers of ranitidine N- and S-oxides [9].
  • The S-oxidation of M2 by recombinant human FMO5 was not appreciably inhibited in the presence of methimazole [8].
  • 5. The present results suggest that the S-oxidation of S-methyl esonarimod reflects FMO5 activity in the human liver because the recombinant FMO5 data match well with the human liver microsomal experiments [8].
  • Purified mini-pig liver FMO1, rabbit lung FMO2, and human cDNA-expressed FMO3 efficiently oxidized sulindac sulfide with a high degree of stereoselectivity towards the R-isomer, but FMO5 lacked catalytic activity [10].
  • Prochiral sulfoxidation of probe compounds based on p-tolyl methyl sulfide is a particularly useful method for discriminating among FMO1, FMO3, and FMO5, because the stereochemistry of the resulting products is isoform dependent, but apparently species independent [11].

Other interactions of FMO5

  • Of the individuals analysed, all contained CYP2B6 mRNA in their skin, 90% contained FMO5 mRNA and about half contained mRNAs encoding FMOs 1, 3, and 4, and CYPs 2A6 and 3A4 [7].
  • 3. Recombinant human FMO1 and FMO5 produced M3 in greater quantities than recombinant human FMO3 [8].
  • Relapse-free survival was longer among patients with FMO5-overexpressing tumors or NAT1-overexpressing tumors (P = 0.0066 and P = 0.000052, respectively), but only NAT1 status retained prognostic significance in Cox multivariate regression analysis (P = 0.0013) [12].


  1. Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Overby, L.H., Buckpitt, A.R., Lawton, M.P., Atta-Asafo-Adjei, E., Schulze, J., Philpot, R.M. Arch. Biochem. Biophys. (1995) [Pubmed]
  2. Alternative processing events in human FMO genes. Lattard, V., Zhang, J., Cashman, J.R. Mol. Pharmacol. (2004) [Pubmed]
  3. Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Hines, R.N., Hopp, K.A., Franco, J., Saeian, K., Begun, F.P. Mol. Pharmacol. (2002) [Pubmed]
  4. Progesterone regulated expression of flavin-containing monooxygenase 5 by the B-isoform of progesterone receptors: implications for tamoxifen carcinogenicity. Miller, M.M., James, R.A., Richer, J.K., Gordon, D.F., Wood, W.M., Horwitz, K.B. J. Clin. Endocrinol. Metab. (1997) [Pubmed]
  5. A novel flavin-containing monooxygenase from Methylophaga sp strain SK1 and its indigo synthesis in Escherichia coli. Choi, H.S., Kim, J.K., Cho, E.H., Kim, Y.C., Kim, J.I., Kim, S.W. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  6. Physical mapping of the human connexin 40 (GJA5), flavin-containing monooxygenase 5, and natriuretic peptide receptor a genes on 1q21. Gelb, B.D., Zhang, J., Cotter, P.D., Gershin, I.F., Desnick, R.J. Genomics (1997) [Pubmed]
  7. Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450. Janmohamed, A., Dolphin, C.T., Phillips, I.R., Shephard, E.A. Biochem. Pharmacol. (2001) [Pubmed]
  8. S-oxidation of S-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes. Ohmi, N., Yoshida, H., Endo, H., Hasegawa, M., Akimoto, M., Higuchi, S. Xenobiotica (2003) [Pubmed]
  9. Oxidation of ranitidine by isozymes of flavin-containing monooxygenase and cytochrome P450. Chung, W.G., Park, C.S., Roh, H.K., Lee, W.K., Cha, Y.N. Jpn. J. Pharmacol. (2000) [Pubmed]
  10. Stereoselective sulfoxidation of sulindac sulfide by flavin-containing monooxygenases. Comparison of human liver and kidney microsomes and mammalian enzymes. Hamman, M.A., Haehner-Daniels, B.D., Wrighton, S.A., Rettie, A.E., Hall, S.D. Biochem. Pharmacol. (2000) [Pubmed]
  11. Prochiral sulfoxidation as a probe for flavin-containing monooxygenases. Yeung, C.K., Rettie, A.E. Methods Mol. Biol. (2006) [Pubmed]
  12. Relationship between intratumoral expression of genes coding for xenobiotic-metabolizing enzymes and benefit from adjuvant tamoxifen in estrogen receptor alpha-positive postmenopausal breast carcinoma. Bièche, I., Girault, I., Urbain, E., Tozlu, S., Lidereau, R. Breast Cancer Res. (2004) [Pubmed]
WikiGenes - Universities