Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit.
- 1 March 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (3) , 931-935
- https://doi.org/10.1073/pnas.74.3.931
Abstract
.gamma.-Glutamyl transpeptidase, which consists of 2 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 MW 22,000 and 46,000) and the transpeptidase of human kidney (which has subunits of MW 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.This publication has 25 references indexed in Scilit:
- DON, CONV and DONV—I. Inhibition of l-Asparagine synthetase in vitroBiochemical Pharmacology, 1976
- Hydrolysis and transfer reactions catalyzed by γ-glutamyl transpeptidase; Evidence for separate substrate sites and for high affinity of L-cystineBiochemical and Biophysical Research Communications, 1976
- Glutathione and Related γ-Glutamyl Compounds: Biosynthesis and UtilizationAnnual Review of Biochemistry, 1976
- Decrease in glutathione levels of kidney and liver after injection of methionine sulfoximine into ratsBiochemical and Biophysical Research Communications, 1975
- On the Enzymology of Amino Acid TransportScience, 1973
- The AmidotransferasesPublished by Wiley ,1973
- Anthranilate SynthetasePublished by Wiley ,1973
- Half-of-the-sites reactivity and conformational states of cytidine triphosphate synthetaseBiochemistry, 1971
- Computer analysis of the active site of glutamine synthetaseBiochemistry, 1970
- The Specificity of Glutamine Synthetase and Its Relationship to Substrate Conformation at the Active SitePublished by Wiley ,1968