γ-Glutamyl transpeptidase in hydra

J. Danner, H. M. Lenhoff, M. Houston-Cobb, W. Heagy, G. R. Marshall

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

γ-Glutamyl transpeptidase (EC 2.3.2.2) activity is described in the coelenterate, Hydra attenuata, using the substrate γ-glutamyl-p-nitroanilide. The properties of the γ-glutamyl donor required for binding to the transpeptidase were investigated by measuring the ability of GSH analogs to inhibit the release of p-nitroaniline. Whereas no binding was observed when the γ-glutamyl moiety was altered, analogs with substitution in the Cys residue were capable of binding to the enzyme. A specificity for the Gly residue was indicated because analogs containing Leu or Tyr in place of Gly exhibited decreased binding capacities for the hydra transpeptidase. A comparison of these data with those obtained using the same analogs in the GSH induced feeding response bioassay shows that γ-glutamyl transpeptidase activity and the GSH receptor for the hydra feeding response have different specificities.

Original languageEnglish (US)
Pages (from-to)180-186
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume73
Issue number1
DOIs
StatePublished - Nov 8 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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