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Gene Review

gor  -  glutathione oxidoreductase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3485, JW3467, gorA
 
 
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Disease relevance of gor

  • Seven independently isolated glutathione reductase-deficient (gor) Escherichia coli mutants were found to have an in vivo glutathione redox state that did not significantly differ from that of the parental strain, 98 to 99% reduced [1].
  • Interestingly, its expression and enzyme characteristics were different from GR homologue of filarial parasite O. volvulus [2].
 

High impact information on gor

  • Moreover, Grx1 could catalyze disulfide formation in the oxidizing cytosol of combined null mutants for glutathione reductase and thioredoxin 1. grxB(-) cells were more sensitive to hydrogen peroxide and other oxidants and showed increased carbonylation of intracellular proteins, particularly in the stationary phase [3].
  • Human thioredoxin reductase is a pyridine nucleotide-disulfide oxidoreductase closely related to glutathione reductase but differing from the latter in having a Cys-SeCys (selenocysteine) sequence as an additional redox center [4].
  • These results identify His509 as active site base, but imply that its function can be substituted, although inefficiently, by an alternative proton donor, similar to glutathione reductase [5].
  • A scheme is described for the large scale purification of thioredoxin, thioredoxin reductase, and glutathione reductase [6].
  • Thioredoxin reductase contains FAD and NADPH binding domains that are structurally similar to the corresponding domains of the related enzyme glutathione reductase [7].
 

Chemical compound and disease context of gor

 

Biological context of gor

 

Anatomical context of gor

 

Associations of gor with chemical compounds

 

Regulatory relationships of gor

  • In sodA mutant cells lacking manganese superoxide dismutase activity but expressing the cloned gor gene (QC772:pJIK1) increased cellular glutathione reductase activity did not provide protection against methylviologen [10].
 

Other interactions of gor

 

Analytical, diagnostic and therapeutic context of gor

References

  1. Glutathione reductase is not required for maintenance of reduced glutathione in Escherichia coli K-12. Tuggle, C.K., Fuchs, J.A. J. Bacteriol. (1985) [Pubmed]
  2. Environmental stressors (salinity, heavy metals, H(2)O(2)) modulate expression of glutathione reductase (GR) gene from the intertidal copepod Tigriopus japonicus. Seo, J.S., Lee, K.W., Rhee, J.S., Hwang, D.S., Lee, Y.M., Park, H.G., Ahn, I.Y., Lee, J.S. Aquat. Toxicol. (2006) [Pubmed]
  3. Characterization of Escherichia coli null mutants for glutaredoxin 2. Vlamis-Gardikas, A., Potamitou, A., Zarivach, R., Hochman, A., Holmgren, A. J. Biol. Chem. (2002) [Pubmed]
  4. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. Gromer, S., Arscott, L.D., Williams, C.H., Schirmer, R.H., Becker, K. J. Biol. Chem. (1998) [Pubmed]
  5. Identification and characterization of the functional amino acids at the active site of the large thioredoxin reductase from Plasmodium falciparum. Gilberger, T.W., Walter, R.D., Müller, S. J. Biol. Chem. (1997) [Pubmed]
  6. Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. Pigiet, V.P., Conley, R.R. J. Biol. Chem. (1977) [Pubmed]
  7. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. Waksman, G., Krishna, T.S., Williams, C.H., Kuriyan, J. J. Mol. Biol. (1994) [Pubmed]
  8. Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Greer, S., Perham, R.N. Biochemistry (1986) [Pubmed]
  9. Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant. Mittl, P.R., Berry, A., Scrutton, N.S., Perham, R.N., Schulz, G.E. J. Mol. Biol. (1993) [Pubmed]
  10. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Kunert, K.J., Cresswell, C.F., Schmidt, A., Mullineaux, P.M., Foyer, C.H. Arch. Biochem. Biophys. (1990) [Pubmed]
  11. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Mittl, P.R., Schulz, G.E. Protein Sci. (1994) [Pubmed]
  12. Unique organization of the dnaA region from Prochlorococcus marinus CCMP1375, a marine cyanobacterium. Richter, S., Hess, W.R., Krause, M., Messer, W. Mol. Gen. Genet. (1998) [Pubmed]
  13. Role of glutathione in the response of Escherichia coli to osmotic stress. Smirnova, G.V., Krasnykh, T.A., Oktyabrsky, O.N. Biochemistry Mosc. (2001) [Pubmed]
 
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