Continuation of studies are proposed on the mechanisms of the reactions catalyzed by and on the structure-function relationships involved in the regulation of glutamine synthetases, gamma-glutamyl cysteine synthetase, 5-oxo-L-prolinase, gamma-glutamyl transpeptidase, gamma-glutamyl cyclotransferase, glutamine-dependent carbamyl phosphate synthetase, glutamate synthase, aspartate beta-decarboxylase, and related enzymes. The enzymes will be purified and characterized by physical and chemical studies as well as by investigations of their catalytic behavior. Further insights into the relationships between the enzyme-catalyzed reactions and physiological phenomena will be sought.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM012034-19
Application #
3150816
Study Section
Biochemistry Study Section (BIO)
Project Start
1977-09-01
Project End
1987-08-31
Budget Start
1985-09-01
Budget End
1986-08-31
Support Year
19
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Weill Medical College of Cornell University
Department
Type
Schools of Medicine
DUNS #
201373169
City
New York
State
NY
Country
United States
Zip Code
10065
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Li, L Y; Seddon, A P; Meister, A (1987) 18O studies on the 5-oxoprolinase reaction. Evidence for a phosphorylated tetrahedral intermediate. J Biol Chem 262:11020-5
Simondsen, R P; Meister, A (1986) Interaction of the D-isomer of gamma-methylene glutamate with an active site thiol of gamma-glutamylcysteine synthetase. J Biol Chem 261:17134-7
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