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Clinical Chemistry 25: 75-79, 1979;
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Clinical Chemistry, Vol 25, 75-79, Copyright © 1979 by American Association for Clinical Chemistry

Hydrolysis of glutathione by human liver gamma-glutamyltransferase

LM Shaw and DA Newman

We studied the catalytic hydrolysis of glutathione by human liver gamma- glutamyltransferase [(gamma-glutamyl)-peptide:amino acid gamma- glutamyltransferase, EC 2.3.2.2]. Glutamate production from glutathione was maximal at pH 7.4 (37 degrees C). Kinetically, the liver enzyme is similar to human kidney gamma-glutamyltransferase: their respective Km values with glutathione as substrate are similar (0.096 x 10(-3) mol/L and 0.097 x 10(-3) mol/L, respectively). S-Methylglutathione was hydrolyzed at a slightly higher rate than glutatione by liver gamma- glutamyltransferase. From these findings and other established properties of liver and kidney gamma-glutamyltransferase we propose that human liver is an important site of glutathione catabolism and that gamma-glutamyltransferase in liver catalyzes the first step of the catabolism of glutathione and glutathione conjugates in this organ.


The following articles in journals at HighWire Press have cited this article:


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P. Giral, N. Jacob, C. Dourmap, B. Hansel, A. Carrie, E. Bruckert, X. Girerd, and M. J. Chapman
Elevated Gamma-Glutamyltransferase Activity and Perturbed Thiol Profile Are Associated With Features of Metabolic Syndrome
Arterioscler. Thromb. Vasc. Biol., March 1, 2008; 28(3): 587 - 593.
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Copyright © 1979 by the American Association for Clinical Chemistry.