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Gene Review

FMO1  -  Fmo1p

Saccharomyces cerevisiae S288c

Synonyms: Flavin-dependent monooxygenase, Thiol-specific monooxygenase, YHR176W
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Disease relevance of FMO1

  • The properties of FMO3 cDNA expressed in Escherichia coli were found to be more similar to those of FMO1 than FMO2, but to differ significantly from both [1].

High impact information on FMO1

  • The FMO1 gene appears to be under control of an unfolded protein response element and is inducible by factors, such as reductive stress, that elicit the unfolded protein response [2].
  • The ubiF gene encodes a flavin-dependent monooxygenase that shares no homology to the Coq7 protein and is required for the final monooxygenase step of Q biosynthesis in E. coli [3].
  • Based on sequence homology to known proteins, we suggest that COQ6 encodes a flavin-dependent monooxygenase required for one or more steps in Q biosynthesis [4].
  • Of these, 117 clones remained under high stringency hybridization conditions (65 degrees C, 50% formamide, 0.1 x SSC, 0.1% SDS) and were identified as FMO1 (95 clones) or FMO5 (22 clones) [1].
  • A cDNA library was constructed from rabbit liver mRNA and screened under low stringency hybridization conditions (30 degrees C, 50% formamide, 1 x SSC, 0.1% SDS) with the mixture of 5' FMO1, FMO2, and FMO5 cDNA probes [1].

Biological context of FMO1


Anatomical context of FMO1

  • RNA blot analysis showed that the mouse FMO1 was also expressed in the lung and kidney and to lesser extents in the heart, spleen, testis and brain [5].

Associations of FMO1 with chemical compounds


Analytical, diagnostic and therapeutic context of FMO1


  1. Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3. Burnett, V.L., Lawton, M.P., Philpot, R.M. J. Biol. Chem. (1994) [Pubmed]
  2. Yeast flavin-containing monooxygenase is induced by the unfolded protein response. Suh, J.K., Robertus, J.D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  3. Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis. Tran, U.C., Marbois, B., Gin, P., Gulmezian, M., Jonassen, T., Clarke, C.F. J. Biol. Chem. (2006) [Pubmed]
  4. The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis. Gin, P., Hsu, A.Y., Rothman, S.C., Jonassen, T., Lee, P.T., Tzagoloff, A., Clarke, C.F. J. Biol. Chem. (2003) [Pubmed]
  5. Molecular cloning of mouse liver flavin containing monooxygenase (FMO1) cDNA and characterization of the expression product: metabolism of the neurotoxin, 1,2,3,4-tetrahydroisoquinoline (TIQ). Itoh, K., Nakamura, K., Kimura, T., Itoh, S., Kamataki, T. The Journal of toxicological sciences. (1997) [Pubmed]
  6. Redox regulation of yeast flavin-containing monooxygenase. Suh, J.K., Poulsen, L.L., Ziegler, D.M., Robertus, J.D. Arch. Biochem. Biophys. (2000) [Pubmed]
  7. Determination of FAD-binding domain in flavin-containing monooxygenase 1 (FMO1). Kubo, A., Itoh, S., Itoh, K., Kamataki, T. Arch. Biochem. Biophys. (1997) [Pubmed]
  8. Molecular cloning and characterization of a full-length flavin-dependent monooxygenase from yeast. Zhang, M., Robertus, J.D. Arch. Biochem. Biophys. (2002) [Pubmed]
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