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Gstm2  -  glutathione S-transferase mu 2

Rattus norvegicus

Synonyms: GST 4-4, GST Yb2, GSTM2-2, Glutathione S-transferase Mu 2, Glutathione S-transferase Yb-2
 
 
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Disease relevance of Gstm2

 

High impact information on Gstm2

 

Biological context of Gstm2

  • We conclude that the GSTs account for the major portion of GTN biotransformation in rat aortic cytosol, and that this is primarily attributable to the GST Yb2 isoform [4].
  • The substrate specificity and stereoselectivity of GST 4-4 are most likely determined by pIS1 and the distance between the site of GSH attack and Lewis base atoms in the substrates which interact with either pIS2, pIS3, or a combination of these sites [5].
 

Associations of Gstm2 with chemical compounds

 

Analytical, diagnostic and therapeutic context of Gstm2

References

  1. Reduced expression of glutathione S-transferase Yb2 during progression of chemically induced hepatocellular carcinomas in Fischer 344 rats. Stalker, M.J., Kocal, T.E., Quinn, B.A., Gordon, S.G., Hayes, M.A. Hepatology (1994) [Pubmed]
  2. Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate. Hornby, J.A., Luo, J.K., Stevens, J.M., Wallace, L.A., Kaplan, W., Armstrong, R.N., Dirr, H.W. Biochemistry (2000) [Pubmed]
  3. A homology model for rat mu class glutathione S-transferase 4-4. de Groot, M.J., Vermeulen, N.P., Mullenders, D.L., Donné-Op den Kelder, G.M. Chem. Res. Toxicol. (1996) [Pubmed]
  4. Isoform-specific biotransformation of glyceryl trinitrate by rat aortic glutathione S-transferases. Nigam, R., Anderson, D.J., Lee, S.F., Bennett, B.M. J. Pharmacol. Exp. Ther. (1996) [Pubmed]
  5. A predictive substrate model for rat glutathione S-transferase 4-4. de Groot, M.J., van der Aar, E.M., Nieuwenhuizen, P.J., van der Plas, R.M., Donné-Op den Kelder, G.M., Commandeur, J.N., Vermeulen, N.P. Chem. Res. Toxicol. (1995) [Pubmed]
  6. Glutathione conjugation of microsome-mediated and synthetic aflatoxin B1-8,9-oxide by purified glutathione S-transferases from rats. Gopalan, P., Jensen, D.E., Lotlikar, P.D. Cancer Lett. (1992) [Pubmed]
  7. In vitro and in vivo reversible and irreversible inhibition of rat glutathione S-transferase isoenzymes by caffeic acid and its 2-S-glutathionyl conjugate. Ploemen, J.H., van Ommen, B., de Haan, A., Schefferlie, J.G., van Bladeren, P.J. Food Chem. Toxicol. (1993) [Pubmed]
 
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