Gene Symbol: gor
Description: glutathione oxidoreductase
Alias: ECK3485, JW3467, gorA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     gor

Top Publications

  1. Deonarain M, Scrutton N, Berry A, Perham R. Directed mutagenesis of the redox-active disulphide bridge in glutathione reductase from Escherichia coli. Proc Biol Sci. 1990;241:179-86 pubmed
    Directed mutagenesis of the gor gene from Escherichia coli encoding the flavoprotein glutathione reductase was used to convert the two cysteine residues that comprise its redox-active disulphide bridge to alanine (C42A) and serine (C47S) ..
  2. Toledano M, Kumar C, Le Moan N, Spector D, Tacnet F. The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis. FEBS Lett. 2007;581:3598-607 pubmed
    ..We show that although prokaryotic and eukaryotic systems have a similar architecture, they profoundly differ in their overall cellular functions. ..
  3. Lillig C, Potamitou A, Schwenn J, Vlamis Gardikas A, Holmgren A. Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins. J Biol Chem. 2003;278:22325-30 pubmed
    ..Escherichia coli lacking glutathione reductase and glutaredoxins (gor-grxA-grxB-grxC-) barely grows on sulfate...
  4. Waldman H. Baby fat is cute, but chubby kids may be in danger. ASDC J Dent Child. 2000;67:15-7, 8 pubmed
    ..An increasing percent of children are overweight. A review of the prevalence of overweight children in different demographic groups is provided in an effort to alert dentists to the role they could play in preventing medical complications. ..
  5. Mittl P, Schulz G. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci. 1994;3:799-809 pubmed
    ..coli enzyme accepts trypanothione much better than the human enzyme. The reported structure provides a frame for explaining numerous published engineering results in detail and for guiding further ones. ..
  6. Harrison J, Tremaroli V, Stan M, Chan C, Vacchi Suzzi C, Heyne B, et al. Chromosomal antioxidant genes have metal ion-specific roles as determinants of bacterial metal tolerance. Environ Microbiol. 2009;11:2491-509 pubmed publisher
    ..This characterized approximately 250 gene-metal combinations and identified that sodA, sodB, gor, trxA, gshA, grxA and marR have distinct roles in safeguarding or sensitizing cells to different toxic metal ions (..
  7. Faulkner M, Veeravalli K, Gon S, Georgiou G, Beckwith J. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci U S A. 2008;105:6735-40 pubmed publisher
    ..Double mutants lacking thioredoxin reductase (trxB) and glutathione reductase (gor) or glutathione biosynthesis (gshA) cannot grow...
  8. Knapp K, Swartz J. Evidence for an additional disulfide reduction pathway in Escherichia coli. J Biosci Bioeng. 2007;103:373-6 pubmed
    ..However, significant glutathione reductase activity remained. The unknown glutathione reductase pathway is disabled by iodoacetamide, is inhibited by NADH, and appears to use NADPH as an electron source. ..
  9. Gon S, Faulkner M, Beckwith J. In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli. Antioxid Redox Signal. 2006;8:735-42 pubmed
    ..These findings indicate a role for these enzymes either for NrdDG reactivation or some other essential anaerobic process. ..

More Information


  1. Smirnova G, Muzyka N, Oktyabrsky O. Effects of cystine and hydrogen peroxide on glutathione status and expression of antioxidant genes in Escherichia coli. Biochemistry (Mosc). 2005;70:926-34 pubmed
    ..8 to 3.6). The same treatment of cells with deficiency in glutathione oxidoreductase (GOR) resulted in even more severe oxidation of GSH(out), so that the level of oxidized glutathione exceeded that of ..
  2. Greer S, Perham R. Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Biochemistry. 1986;25:2736-42 pubmed
    A glutathione reductase negative strain of Escherichia coli K-12 was isolated as a thermoresistant survivor when a gor::MuctsAp lysogen was subjected to elevated temperature...
  3. Becker Hapak M, Eisenstark A. Role of rpoS in the regulation of glutathione oxidoreductase (gor) in Escherichia coli. FEMS Microbiol Lett. 1995;134:39-44 pubmed
    ..While it is known that in the exponential phase, OxyR is the transcriptional regulator of gor, this study has shown that RpoS regulates gor in the stationary phase...
  4. Bessette P, Aslund F, Beckwith J, Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci U S A. 1999;96:13703-8 pubmed
    ..However, mutants in which the reduction of both thioredoxins and glutathione is impaired (trxB gor mutants) accumulate oxidized, enzymatically active alkaline phosphatase in the cytoplasm...
  5. Smirnova G, Krasnykh T, Oktyabrsky O. Role of glutathione in the response of Escherichia coli to osmotic stress. Biochemistry (Mosc). 2001;66:973-8 pubmed
    The growth of Escherichia coli mutants deficient in glutathione synthesis (gshA) and in glutathione reductase (gor) was suppressed in medium of elevated osmolarity...
  6. Elvin C, Dixon N, Rosenberg H. Molecular cloning of the phosphate (inorganic) transport (pit) gene of Escherichia coli K12. Identification of the pit+ gene product and physical mapping of the pit-gor region of the chromosome. Mol Gen Genet. 1986;204:477-84 pubmed
    ..coli genes inserted in the cosmid vector pHC79. A 25.5-kb chromosomal DNA fragment was shown also to carry the gor locus encoding glutathione oxidoreductase...
  7. Saejung W, Puttikhunt C, Prommool T, Sojikul P, Tanaka R, Fujiyama K, et al. Enhancement of recombinant soluble dengue virus 2 envelope domain III protein production in Escherichia coli trxB and gor double mutant. J Biosci Bioeng. 2006;102:333-9 pubmed
    ..of the soluble protein could be attributed to the thioredoxin reductase (trxB) and glutathione reductase (gor) double mutations in the Origami genome...
  8. Davis N, Greer S, Jones Mortimer M, Perham R. Isolation and mapping of glutathione reductase-negative mutants of Escherichia coli K12. J Gen Microbiol. 1982;128:1631-4 pubmed
    ..Similarly, the prophage site and malA were cotransduced by T4GT7 but not by P1. The gor gene maps between min 77 and 78 on the E. coli genome, and the mutation causes no growth defect.
  9. Pigiet V, Conley R. Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. J Biol Chem. 1977;252:6367-72 pubmed
    ..Both reductases exhibit an absorption band at approximately 320 nm which appears due to a residual amount of tightly bound NADP. Presence of this absorption band has no apparent effect on the specific activity of either enzyme. ..
  10. Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci U S A. 1976;73:2275-9 pubmed
    ..These results demonstrate the existence of two different electron transfer systems from NADPH to deoxyribonucleotides and provide a function for glutathione in DNA synthesis. ..
  11. Mata A, Pinto M, Lopez Barea J. Purification by affinity chromatography of glutathione reductase (EC from Escherichia coli and characterization of such enzyme. Z Naturforsch C. 1984;39:908-15 pubmed
    ..The enzyme was inactivated by low concentrations of para-hydroximercuribenzoate; the sensitivity towards such mercurial was greatly enhanced after reduction of the enzyme by NADPH. ..
  12. Argyrou A, Blanchard J. Flavoprotein disulfide reductases: advances in chemistry and function. Prog Nucleic Acid Res Mol Biol. 2004;78:89-142 pubmed
    ..Selection of the particular nonflavin redox center and utilization of a second, or even a third, nonflavin redox center in some cases presumably represents the most efficient strategy for reduction of the individual substrate. ..
  13. Xiong S, Wang Y, Ren X, Li B, Zhang M, Luo Y, et al. Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant. World J Gastroenterol. 2005;11:1077-82 pubmed
    ..Modification of the redox environment of E. coli cytoplasm can significantly improve the folding of recombinant disulfide-bonded proteins produced in it. ..
  14. Kunert K, Cresswell C, Schmidt A, Mullineaux P, Foyer C. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Arch Biochem Biophys. 1990;282:233-8 pubmed
    ..reductase and glutathione in Escherichia coli the coding sequence of the bacterial glutathione reductase gene (gor gene) was cloned into the vector pBR322, and the gor gene was expressed under the control of the promoter of the ..
  15. Ermler U, Schulz G. The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution. Proteins. 1991;9:174-9 pubmed
    ..coli enzyme was tackled in order to understand site-directed mutants, the most spectacular of which changed the cofactor specificity of this enzyme from NADP to NAD (Scrutton et al., 1990, Nature 343:38-43). ..