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Glutathione metabolism in relation to the amino-acid permeation systems of the yeast Saccharomyces cerevisiae. Occurrence of gamma-glutamyltranspeptidase: its regulation and the effects of permeation mutations on the enzyme cellular level.

par Penninckx, Michel ;Jaspers, Charles ;Wiame, Jean-Marie
Référence European journal of biochemistry / FEBS, 104, 1, page (119-123)
Publication Publié, 1980-02

Article révisé par les pairs

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Résumé :

A careful enzyme specificity analysis has revealed the presence of a typical gamma-glutamyltranspeptidase in the yeast Saccharomyces cerevisiae. The enzyme cellular level is low in the presence of NH4+ as a sole nitrogen source and rises when individual amino acids are used as nitrogen sources. The gamma-glutamyltranspeptidase appears to be repressed by NH+4 and escapes to the regulatory circuits under the control of glutamine and the glutamate-dehydrogenase . NH+4 complex. The transpeptidase cellular level is unaffected in mutants which have lost the general amino acid permease and specific systems for L-arginine and L-lysine. In contrast, a low enzyme level is observed when growing an apf mutant on urea; this mutant is most probably affected in a common element shared by all the amino acid permeation systems. Urea appears to be a nitrogen source which promotes a high transpeptidase level in the wild-type strain. The reported data are discussed in the light of the current theories about the intervention of glutathione metabolism in the translocation of amino acids.