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Gene Review

fre  -  FMN reductase

Escherichia coli O157:H7 str. Sakai

Synonyms: fadI, ubiB
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  1. Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex. Vallurupalli, P., Kay, L.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Analysis of rdxA and involvement of additional genes encoding NAD(P)H flavin oxidoreductase (FrxA) and ferredoxin-like protein (FdxB) in metronidazole resistance of Helicobacter pylori. Kwon, D.H., El-Zaatari, F.A., Kato, M., Osato, M.S., Reddy, R., Yamaoka, Y., Graham, D.Y. Antimicrob. Agents Chemother. (2000) [Pubmed]
  3. Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744. Zenno, S., Saigo, K., Kanoh, H., Inouye, S. J. Bacteriol. (1994) [Pubmed]
  4. Cloning and characterization of genes from Agrobacterium sp. IP I-671 involved in hydantoin degradation. Hils, M., Münch, P., Altenbuchner, J., Syldatk, C., Mattes, R. Appl. Microbiol. Biotechnol. (2001) [Pubmed]
  5. A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor. Valton, J., Filisetti, L., Fontecave, M., Nivière, V. J. Biol. Chem. (2004) [Pubmed]
  6. FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase. Louie, T.M., Yang, H., Karnchanaphanurach, P., Xie, X.S., Xun, L. J. Biol. Chem. (2002) [Pubmed]
  7. The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides. Nivière, V., Fieschi, F., Dećout, J.L., Fontecave, M. J. Biol. Chem. (1999) [Pubmed]
  8. Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. Evidence for the catalytic role of serine 49 residue. Nivière, V., Fieschi, F., Décout, J.L., Fontecave, M. J. Biol. Chem. (1996) [Pubmed]
  9. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals. Gaudu, P., Touati, D., Nivière, V., Fontecave, M. J. Biol. Chem. (1994) [Pubmed]
  10. NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein. Inouye, S. FEBS Lett. (1994) [Pubmed]
  11. Stereospecificity of hydride transfer and substrate specificity for FMN-containing NAD(P)H-flavin oxidoreductase from the luminescent bacterium, Vibrio fischeri ATCC 7744. Inouye, S., Nakamura, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  12. Cys5 and Cys214 of NAD(P)H:flavin oxidoreductase from Escherichia coli are located in the active site. Fieschi, F., Nivière, V., Fontecave, M. Eur. J. Biochem. (1996) [Pubmed]
  13. Frame-shift mutations in NAD(P)H flavin oxidoreductase encoding gene (frxA) from metronidazole resistant Helicobacter pylori ATCC43504 and its involvement in metronidazole resistance. Kwon, D.H., Kato, M., El-Zaatari, F.A., Osato, M.S., Graham, D.Y. FEMS Microbiol. Lett. (2000) [Pubmed]
  14. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. Fontecave, M., Eliasson, R., Reichard, P. J. Biol. Chem. (1987) [Pubmed]
  15. Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Louie, T.M., Xie, X.S., Xun, L. Biochemistry (2003) [Pubmed]
  16. Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. Spyrou, G., Haggård-Ljungquist, E., Krook, M., Jörnvall, H., Nilsson, E., Reichard, P. J. Bacteriol. (1991) [Pubmed]
  17. Identification of the gene encoding a NAD(P)H-flavin oxidoreductase coupling with dibenzothiophene (DBT)-desulfurizing enzymes from the DBT-nondesulfurizing bacterium Paenibacillus polymyxa A-1. Ishii, Y., Ohshiro, T., Aoi, Y., Suzuki, M., Izumi, Y. J. Biosci. Bioeng. (2000) [Pubmed]
  18. The function of superoxide dismutase during the enzymatic formation of the free radical of ribonucleotide reductase. Fontecave, M., Gräslund, A., Reichard, P. J. Biol. Chem. (1987) [Pubmed]
  19. Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli. Gao, B., Bertrand, A., Boles, W.H., Ellis, H.R., Mallett, T.C. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
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