Genomes and Genes
Gene Symbol: gor
Description: glutathione oxidoreductase
Alias: ECK3485, JW3467, gorA
Species: Escherichia coli str. K-12 substr. MG1655
- 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 ..
- 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 pubmedA 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...
- 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...
- 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...
- Smirnova G, Krasnykh T, Oktyabrsky O. Role of glutathione in the response of Escherichia coli to osmotic stress. Biochemistry (Mosc). 2001;66:973-8 pubmedThe growth of Escherichia coli mutants deficient in glutathione synthesis (gshA) and in glutathione reductase (gor) was suppressed in medium of elevated osmolarity...
- 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...
- 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...
- 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.
- 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. ..
- 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. ..
- Mata A, Pinto M, Lopez Barea J. Purification by affinity chromatography of glutathione reductase (EC 220.127.116.11) 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. ..
- 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. ..
- 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. ..
- 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 ..
- 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). ..