Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae
1985; Elsevier BV; Volume: 24; Issue: 4 Linguagem: Inglês
10.1016/s0031-9422(00)84880-3
ISSN1873-3700
AutoresCharles Jaspers, Daniel Gigot, Michel Pennînckx,
Tópico(s)Advanced Glycation End Products research
ResumoThe 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.
Referência(s)