Dipeptide-hydroxamates are good inhibitors of the angiotensin I-converting enzyme.
The inhibition constants (Ki) and modes of inhibition have been determined for a series of dipeptide-hydroxamate compounds with bovine lung parenchyma angiotensin I-converting enzyme (peptidyldipeptide carboxy-hydrolase, E.C. 3.4. 15.1). The hydroxamido function was borne by aspartic, glutamic, or aminoadipic acid and extended by 2, 3 or 4 bond lengths from the proline amide bond. L-glu(NHOH)-L-pro (Ki = 3.4 microM) and D,L-aminoadipicyl (NHOH)-L-pro (Ki = 1.2 microM) were the best competitive inhibitors of the hydrolysis of benzoyl-gly-his-gly but were not effective as affinity ligands for purification of the enzyme.
D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D002417:Cattle; D006877:Hydroxamic Acids / Q000494:pharmacology*; D008168:Lung / Q000201:enzymology; D010455:Peptides / Q000494:pharmacology*
D000806:Angiotensin-Converting Enzyme Inhibitors; D006877:Hydroxamic Acids; D010455:Peptides