Conversion of glutathione to glutathione disulfide, a catalytic function of gamma-glutamyl transpeptidase.
نویسندگان
چکیده
منابع مشابه
Gama-Glutamyl Transpeptidase and Glutathione Function
γ-Glutamyl transpeptidase (5-L-glutamyl-peptide: amino acid 5-glutamyl transferase; EC 2.3.2.2; abbreviated GGT), is a plasma membrane-associated enzyme that is located on the outer surface of the cells of secretory tissues [1]. It plays a central role in the metabolism of glutathione that is widely in various mammals [2]. The enzyme catalyzes the degradation of the extracellular glutathione in...
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The degradation pathway of glutathione (GSH) in plants is not well understood. In mammals, GSH is predominantly metabolized through the gamma-glutamyl cycle, where GSH is degraded by the sequential reaction of gamma-glutamyl transpeptidase (GGT), gamma-glutamyl cyclotransferase, and 5-oxoprolinase to yield glutamate (Glu) and dipeptides that are subject to peptidase action. In this study, we ex...
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In a previous publication (1) methods were described which permit the quantitative estimation of the action of y-glutamyl transpeptidase upon glutathione. In the present report these methods are employed to study the influence of amino acids. pcptides, and other compounds upon the reaction. In addition, we present the results of attempts to account for all the main products formed in the reacti...
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Gamma-glutamyl transpeptidase, an enzyme of importance in glutathione metabolism, consists of two subunits, one of which (the light subunit, Mr 22,000; residues 380-568; rat kidney) contains residue Thr-523, which selectively interacts with the substrate analog acivicin to form an adduct that is apparently analogous to the gamma-glutamyl enzyme intermediate formed in the normal reaction (Stole,...
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Inhibitors for glutathione S-transferase (GST) iso-enzymes from rat liver with high affinity for the glutathione-binding site (G-site) have been developed. In previous studies, a model was described for the G-site of GST (Adang, A. E. P., Brussee, J., van der Gen, A., and Mulder, G. J. (1990) Biochem. J. 269, 47-54) in terms of essential and nonessential interactions between groups in glutathio...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50446-4