Characterization of extracellular γ-glutamyl transpeptidase from Aspergillus nidulans

Zsolt Spitzmüller, Sándor Gonda, Attila Kiss-Szikszai, G. Vasas, I. Pócsi, T. Emri

Research output: Contribution to journalArticle


Aspergillus nidulans γ-glutamyl transpeptidase (AnγGT, EC was partially purified from the fermentation broth of carbon stressed cultures. Its temperature and pH optimum was 45 °C and pH 8.0, respectively. AnγGT had little hydrolase activity. It utilized Gln, glutathione and less efficiently oxidized glutathione as γ-glutamyl donors (beside of γ-glutamyl-p-nitroanilide) and amino-acids and peptides (including Glu, Cys, Met, Gly-Gly and Cys-Gly) but not hydroxylamine as γ-glutamyl acceptors. We propose that the function of this enzyme is not to degrade, but to produce, γ-glutamyl compounds which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures.

Original languageEnglish
Pages (from-to)400-403
Number of pages4
Issue number6
Publication statusPublished - Nov 1 2016


  • Carbon stress
  • Glutathione metabolism
  • Utilization of peptides
  • γ-Glutamyl transpeptidase substrates

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics

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