Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae
Abstract
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- info:eu-repo/semantics/article
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- Biologie moléculaire
- Horticulture
- Biochimie
- Botanique générale
- amino acid uptake
- glutathione
- glutathione turnover
- Saccharomyces cerevisiae
- transpeptidation.
- yeast
- γ-glutamyl cycle
- γ-glutamyl peptides
- γ-glutamyltranspeptidase