Purine and pyrimidine inhibitors of arginase.
1. Adenosine, inosine, adenine and uric acid are competitive inhibitors and cytidine and cytosine noncompetitive inhibitors of bovine liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1). 2. The affinity of the enzyme for these inhibitors was 10--100 times as great as for substrate in terms of Ki versus Km. 3. These nucleic acid metabolites may thus function in vivo to regulate the urea cycle. 4. Several naturally occuring competitive and noncompetitive inhibitors of arginase of unknown structure have been isolated from plant and animal tissue. From their properties and methods of isolation, they may be the purines and pyrimidines herein described. 5. These purines and pyrimidines have no effect on tryptic hydrolysis.
D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors*; D001667:Binding, Competitive; D002417:Cattle; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011687:Purines / Q000494:pharmacology*; D011743:Pyrimidines / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D011687:Purines; D011743:Pyrimidines; D001119:Arginase