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GSH2  -  glutathione synthase

Saccharomyces cerevisiae S288c

Synonyms: GSH synthetase, GSH-S, Glutathione synthase, Glutathione synthetase, YOL049W
 
 
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Disease relevance of GSH2

  • In the present report, we show that crude extracts of Streptococcus agalactiae catalyze the gamma-GCS and GS reactions and can synthesize GSH from its constituent amino acids [1].
 

High impact information on GSH2

  • GSH is synthesized from its constituent amino acids by two ATP-dependent reactions catalyzed by gamma-glutamylcysteine synthetase and glutathione synthetase [2].
  • Gamma-glutamylcysteine synthetase (gamma-GCS) and glutathione synthetase (GS), distinct enzymes that together account for glutathione (GSH) synthesis, have been isolated and characterized from several Gram-negative prokaryotes and from numerous eukaryotes including mammals, amphibians, plants, yeast, and protozoa [1].
  • This novel bifunctional enzyme, referred to as gamma-GCS-GS, has been characterized in terms of catalytic activity, substrate specificity, and inhibition by GSH, cystamine, and transition state analog sulfoximines [1].
  • The C terminus (360 amino acids) is, however, homologous to D-Ala, D-Ala ligase (24% identity; 38% similarity), an enzyme having the same protein fold as known GS proteins [1].
  • The present study demonstrates that GSH2 expression is also regulated by Yap1p under oxidative stress-induced conditions [3].
 

Chemical compound and disease context of GSH2

 

Biological context of GSH2

 

Anatomical context of GSH2

 

Associations of GSH2 with chemical compounds

 

Other interactions of GSH2

  • Both gsh1 and gsh2 mutants could acquire thermotolerance by mild heat-shock stress and induction of Hsp104p in both mutants was normal; however, mutant cells died faster by heat shock than their parental wild-type strain [12].
  • The gsh2-deficient mutant, which accumulates gamma-glutamylcysteine (an intermediate of glutathione biosynthesis), was also sensitive to methylglyoxal compared with the isogenic wild type strain, although the growth arrest caused by methylglyoxal was partially restored by overexpression of the GLO1 gene [13].
  • Glutathione synthase (GSH1) deletion led to decreased DHA survival in agreement with the glutathione cofactor requirement for the SFA1-encoded activity [14].
 

Analytical, diagnostic and therapeutic context of GSH2

References

  1. Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities. Janowiak, B.E., Griffith, O.W. J. Biol. Chem. (2005) [Pubmed]
  2. Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. Mendoza-Cózatl, D., Loza-Tavera, H., Hernández-Navarro, A., Moreno-Sánchez, R. FEMS Microbiol. Rev. (2005) [Pubmed]
  3. The Yap1p-dependent induction of glutathione synthesis in heat shock response of Saccharomyces cerevisiae. Sugiyama, K., Izawa, S., Inoue, Y. J. Biol. Chem. (2000) [Pubmed]
  4. Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine. Grant, C.M., MacIver, F.H., Dawes, I.W. Mol. Biol. Cell (1997) [Pubmed]
  5. Molecular identification of glutathione synthetase (GSH2) gene from Saccharomyces cerevisiae. Inoue, Y., Sugiyama, K., Izawa, S., Kimura, A. Biochim. Biophys. Acta (1998) [Pubmed]
  6. GSH2, a gene encoding gamma-glutamylcysteine synthetase in the methylotrophic yeast Hansenula polymorpha. Ubiyvovk, V.M., Nazarko, T.Y., Stasyk, O.G., Sohn, M.J., Kang, H.A., Sibirny, A.A. FEMS Yeast Res. (2002) [Pubmed]
  7. Glutathione synthetase from Plasmodium falciparum. Meierjohann, S., Walter, R.D., Müller, S. Biochem. J. (2002) [Pubmed]
  8. Generation of free radicals during the death of Saccharomyces cerevisiae caused by lipid hydroperoxide. Aoshima, H., Kadoya, K., Taniguchi, H., Satoh, T., Hatanaka, H. Biosci. Biotechnol. Biochem. (1999) [Pubmed]
  9. Glutathione regulates the expression of gamma-glutamylcysteine synthetase via the Met4 transcription factor. Wheeler, G.L., Quinn, K.A., Perrone, G., Dawes, I.W., Grant, C.M. Mol. Microbiol. (2002) [Pubmed]
  10. Large conformational changes in the catalytic cycle of glutathione synthase. Gogos, A., Shapiro, L. Structure (Camb.) (2002) [Pubmed]
  11. Anti-glycation defences in yeast. Ponces Freire, A., Ferreira, A., Gomes, R., Cordeiro, C. Biochem. Soc. Trans. (2003) [Pubmed]
  12. Role of glutathione in heat-shock-induced cell death of Saccharomyces cerevisiae. Sugiyama, K., Kawamura, A., Izawa, S., Inoue, Y. Biochem. J. (2000) [Pubmed]
  13. Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae. Inoue, Y., Kimura, A. J. Biol. Chem. (1996) [Pubmed]
  14. Dihydroxyacetone detoxification in Saccharomyces cerevisiae involves formaldehyde dissimilation. Molin, M., Blomberg, A. Mol. Microbiol. (2006) [Pubmed]
  15. Glutathione synthetase: similarities of the proteins from Schizosaccharomyces pombe and Arabidopsis thaliana. Wang, C.L., Oliver, D.J. Biochem. J. (1997) [Pubmed]
 
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