Evidence that transpeptidation is a significant function of gamma-glutamyl transpeptidase.
gamma-Glutamyl transpeptidase (purified from rat kidney) was incubated with glutathione and a mixture of amino acids that closely approximates the amino acid composition of blood plasma, and the relative extents of transpeptidation and hydrolysis were determined by quantitative measurement of the products formed (glutamate, cysteinylglycine, gamma-glutamyl amino acids). At pH 7.4, in the presence of 50 microM glutathione and the amino acid mixture, about 50% of the glutathione that was utilized participated in transpeptidation. Studies in which the formation of individual gamma-glutamyl amino acids was determined in the presence of glutathione and the amino acid mixture showed that L-cystine and L-glutamine are the most active amino acid acceptors, and that other neutral amino acids also participate in transpeptidation to a significant extent. These in vitro experiments are consistent with a number of other findings which indicate that transpeptidation is a significant physiological function of gamma-glutamyl transpeptidase.
D000818:Animals; D004151:Dipeptides / Q000096:biosynthesis; D005978:Glutathione; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D010455:Peptides / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D004151:Dipeptides; D010455:Peptides; D005723:gamma-Glutamyltransferase; D005978:Glutathione