Affinity labeling of γ glutamyl transpeptidase and location of the γ glutamyl binding site on the light subunit Academic Article uri icon

Overview

MeSH Major

  • gamma-Glutamyltransferase

abstract

  • Gamma-Glutamyl transpeptidase, which consists of two nonidentical subunits, is rapidly inactivated with respect to its transpeptidase and hydrolase activities by the gamma-glutamyl analogs 6-diazo-5-oxo-L-norleucine and L-azaserine. Inactivation, which is prevented by gamma-glutamyl substrates (but not by acceptor substrates), is accelerated by maleate, which was previously shown to enhance utilization of glutamine by transpeptidase. 6-Diazo-5-oxo--norleucine reacts specifically, covalently, and stoichiometrically at the gamma-glutamyl site of the enzyme, which was localized through studies with 6-diazo-5-OXO-[14C]norleucine to the light subunits of both the transpeptidase of rat kidney (which has subunits of molecular weights 22,000 and 46,000) and the transpeptidase of human kidney (which has subunits of molecular weights 22,000 and 62,000). The findings, which indicate that these enzymes have similar gamma-glutamyl binding subunits, are relevant to the structure-function relationships of this membrane-bound enzyme and its physiological role.

publication date

  • December 1977

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC430536

PubMed ID

  • 15260

Additional Document Info

start page

  • 931

end page

  • 5

volume

  • 74

number

  • 3