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Gene Review

ECs0046  -  oxidoreductase FixC

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs0046


High impact information on ECs0046


Chemical compound and disease context of ECs0046


Biological context of ECs0046


Anatomical context of ECs0046


Associations of ECs0046 with chemical compounds

  • A BLAST search of protein data bases revealed that PDPr is distantly related to the mitochondrial flavoprotein dimethylglycine dehydrogenase, which functions in choline degradation [21].
  • In addition, three previously identified NPXase segments, known to be involved in FAD and NAD(P)-binding in other pyridine nucleotide-linked flavoprotein oxidoreductases, are strongly conserved in NOXase [3].
  • Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module [22].
  • The recombinant protein was purified by affinity chromatography on guazatine-Sepharose 4B and was shown to be a flavoprotein able to oxidize Spm, norspermine, and N1-acetylspermine with a pH optimum at 8 [23].
  • MTOX forms an anionic flavin semiquinone and a reversible, covalent flavin-sulfite complex (K(d) = 1.7 mM), properties characteristic of flavoprotein oxidases [24].

Other interactions of ECs0046


Analytical, diagnostic and therapeutic context of ECs0046

  • B. amyloliquefaciens YwrO was shown to be a flavoprotein with a monomeric molecular mass of 21.5 kDa by calculation and SDS-PAGE [27].
  • NADPH-cytochrome P450 reductase (CPR) is a membrane-bound flavoprotein that interacts with the membrane via its N-terminal hydrophobic sequence (residues 1-56) [28].
  • In the present work, by replacement of the lysine residue (Lys56) with Gln using site directed mutagenesis, we prepared the full-length flavoprotein mutant Lys56Gln stable to spontaneous proteolysis but possessing spectral and catalytic properties of the wild type flavoprotein [28].


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  11. Multiple states of the Tyr318Leu mutant of dihydroorotate dehydrogenase revealed by single-molecule kinetics. Shi, J., Palfey, B.A., Dertouzos, J., Jensen, K.F., Gafni, A., Steel, D. J. Am. Chem. Soc. (2004) [Pubmed]
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  13. The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors. Zeghouf, M., Fontecave, M., Macherel, D., Covès, J. Biochemistry (1998) [Pubmed]
  14. Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2'-OH Group in Regulating PutA-Membrane Binding(,). Zhang, W., Zhang, M., Zhu, W., Zhou, Y., Wanduragala, S., Rewinkel, D., Tanner, J.J., Becker, D.F. Biochemistry (2007) [Pubmed]
  15. Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase. Ostrowski, J., Barber, M.J., Rueger, D.C., Miller, B.E., Siegel, L.M., Kredich, N.M. J. Biol. Chem. (1989) [Pubmed]
  16. Molecular characterization of the 4'-phosphopantothenoylcysteine decarboxylase domain of bacterial Dfp flavoproteins. Kupke, T. J. Biol. Chem. (2001) [Pubmed]
  17. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. Iverson, T.M., Luna-Chavez, C., Croal, L.R., Cecchini, G., Rees, D.C. J. Biol. Chem. (2002) [Pubmed]
  18. Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean. Kinoshita, T., Emi, T., Tominaga, M., Sakamoto, K., Shigenaga, A., Doi, M., Shimazaki, K. Plant Physiol. (2003) [Pubmed]
  19. Structure and function of a cysBJIH gene cluster in the purple sulphur bacterium Thiocapsa roseopersicina. Haverkamp, T., Schwenn, J.D. Microbiology (Reading, Engl.) (1999) [Pubmed]
  20. The Tricarballylate utilization (tcuRABC) genes of Salmonella enterica serovar Typhimurium LT2. Lewis, J.A., Horswill, A.R., Schwem, B.E., Escalante-Semerena, J.C. J. Bacteriol. (2004) [Pubmed]
  21. Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. Lawson, J.E., Park, S.H., Mattison, A.R., Yan, J., Reed, L.J. J. Biol. Chem. (1997) [Pubmed]
  22. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. Gruez, A., Pignol, D., Zeghouf, M., Covès, J., Fontecave, M., Ferrer, J.L., Fontecilla-Camps, J.C. J. Mol. Biol. (2000) [Pubmed]
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  25. Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions. Becker, D.F., Thomas, E.A. Biochemistry (2001) [Pubmed]
  26. NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein. Inouye, S. FEBS Lett. (1994) [Pubmed]
  27. Bacillus amyloliquefaciens orthologue of Bacillus subtilis ywrO encodes a nitroreductase enzyme which activates the prodrug CB 1954. Anlezark, G.M., Vaughan, T., Fashola-Stone, E., Michael, N.P., Murdoch, H., Sims, M.A., Stubbs, S., Wigley, S., Minton, N.P. Microbiology (Reading, Engl.) (2002) [Pubmed]
  28. Engineering of proteolytically stable NADPH-cytochrome P450 reductase. Bonina, T.A., Gilep, A.A., Estabrook, R.W., Usanov, S.A. Biochemistry Mosc. (2005) [Pubmed]
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