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Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae

By Charles Jaspers, Daniel Gigot and Michel Penninckx


The degradation of glutathione (GSH) in the yeast Saccharomyces cerevisiae appears to be mediated only by γ-glutamyltranspeptidase and cysteinylglycine dipeptidase. Other enzymes of the γ-glutamyl cycle, γ-glutamyl cyclotransferase and 5-oxo-l-prolinase, are not present in the yeast. In vivo transpeptidation was shown in the presence of a high intracellular level of γ-glutamyltranspeptidase, but only when the de-repressing nitrogen source was a suitable acceptor of the transferase reaction. In contrast, when the de-repressing source was not an acceptor of the transferase reaction (e.g. urea), only glutamate was detected. Intracellular GSH is virtually inert when the level of γ-glutamyltranspeptidase is low. Possible roles for in vivo transpeptidation are discussed. © 1985.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Topics: Biologie moléculaire, Horticulture, Biochimie, Botanique générale, amino acid uptake, glutathione, glutathione turnover, Saccharomyces cerevisiae, transpeptidation., yeast, γ-glutamyl cycle, γ-glutamyl peptides, γ-glutamyltranspeptidase
Publisher: 'Elsevier BV'
Year: 1985
DOI identifier: 10.1016/S0031-9422(00)84880-3
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Provided by: DI-fusion
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