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Chemical Compound Review

M4139_SIGMA     2-amino-4-[[1- (carboxymethylcarbamoyl)-2...

Synonyms: AC1MTP80, gamma-glutamyl-S-methylcysteinylglycine
 
 
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High impact information on S-Methylglutathione

  • The same binding in the presence of S-methylglutathione or protoporphyrin IX shows a decreased reaction rate with respect to the reaction in the absence of inhibitors, indicating that the thiols are in proximity of both the glutathione and the porphyrin binding sites [1].
  • The heterodimer is also formed in the presence of S-methylglutathione, but no 1-Cys Prx activity is found under these conditions [2].
  • The acylated product is stable for more than 24 h at pH 7 and 25 degrees C. The modification is reversible in the presence of excess glutathione, but the labeled protein can be protected by adding S-methylglutathione [3].
  • All wild-type enzymes and H107S chimera have nearly identical equilibrium constants for formation of enzyme-GSH complexes (Kd values of 1-2 x 10(-)6 M); however, KmGSH and Ki values for S-methylglutathione inhibition determined by steady-state kinetics are nearly 100-fold higher [4].
  • Subsequent experiments indicated that the inhibitory effects of both glutathione and S-methylglutathione on thiopurine methyltransferase may be due to their acidic natures, changing the reaction mixture pH away from the optimal range for the enzyme [5].
 

Anatomical context of S-Methylglutathione

 

Analytical, diagnostic and therapeutic context of S-Methylglutathione

References

  1. Electron paramagnetic resonance identification of a highly reactive thiol group in the proximity of the catalytic site of human placenta glutathione transferase. Desideri, A., Caccuri, A.M., Polizio, F., Bastoni, R., Federici, G. J. Biol. Chem. (1991) [Pubmed]
  2. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Ralat, L.A., Manevich, Y., Fisher, A.B., Colman, R.F. Biochemistry (2006) [Pubmed]
  3. Programmed delivery of novel functional groups to the alpha class glutathione transferases. Håkansson, S., Viljanen, J., Broo, K.S. Biochemistry (2003) [Pubmed]
  4. Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. Patskovsky, Y.V., Patskovska, L.N., Listowsky, I. Biochemistry (1999) [Pubmed]
  5. Glutathione: an endogenous substrate for thiopurine methyltransferase? Loo, G., Smith, J.T. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  6. Phenotyping of human glutathione S-transferase hGSTT1-1: a comparison of two ex vivo routine procedures. Müller, M., Bünger, J., Voss, M., Westphal, G., Ruhnau, P., Hallier, E. Arch. Toxicol. (2002) [Pubmed]
  7. Analysis of glutathione S-transferase-catalyzed S-alkylglutathione formation by high-performance liquid chromatography. Tracy, J.W., O'Leary, K.A. Anal. Biochem. (1991) [Pubmed]
  8. High-performance liquid chromatography/fluorescence detection of S-methylglutathione formed by glutathione-S-transferase T1 in vitro. Müller, M., Voss, M., Heise, C., Schulz, T., Bünger, J., Hallier, E. Arch. Toxicol. (2001) [Pubmed]
  9. A comparative investigation of the metabolism of methyl bromide and methyl iodide in human erythrocytes. Hallier, E., Deutschmann, S., Reichel, C., Bolt, H.M., Peter, H. International archives of occupational and environmental health. (1990) [Pubmed]
 
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