Abstract
Gamma-glutamyltransferase (GGT), the only enzyme known to initiate the degradative utilization of glutathione (gamma glutamyl-cysteinyl-glycine) is present in the plasma membrane of a number of cell types (14,23). Gammaglutamyltransferase catalyzes the hydrolytic cleavage of the gammaglutamyl linkage in glutathione to form glutamate and cysteinyl-glycine. The latter dipeptide is, in turn, hydrolyzed by dipeptidases to yield cysteine and glycine. In the presence of acceptors of the glutamate molecule, such as cysteine S-S-cysteine (cystine) present in the circulation, the GGT reaction can also yield gammaglutamyl-cystine. Both cysteine and gammaglutamyl-cystine can be re-utilized in the synthesis of glutathione (2,24,29).
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Israel, Y., Nagata, S., Spiesky, H. (1989). Increases in Hepatic Gammaglutamyl Transferase Following Alcohol Consumption. A Hepatoprotective Rather Than a Pathogenic Role. In: Sun, G.Y., Rudeen, P.K., Wood, W.G., Wei, YH., Sun, A.Y. (eds) Molecular Mechanisms of Alcohol. Experimental Biology and Medicine, vol 21. Humana Press. https://doi.org/10.1007/978-1-4612-4514-8_21
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