K-13, a novel inhibitor of angiotensin I converting enzyme produced by Micromonospora halophytica subsp. exilisia. I. Fermentation, isolation and biological properties.
A novel inhibitor of angiotensin I converting enzyme (ACE), designated K-13, was isolated from the culture broth of Micromonospora halophytica subsp. exilisia K-13. K-13 inhibited ACE non-competitively when hippuryl-L-histidyl-L-leucine was used as a substrate. The inhibition constant (Ki) was 0.349 microM. K-13 hardly inhibited carboxypeptidase A, trypsin, alpha-chymotrypsin, leucine aminopeptidase, and aminopeptidase B even at a level of 61 microM. When K-13 was administered intravenously to rats, it inhibited the pressor response to angiotensin I.
D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D007700:Kinetics; D008168:Lung / Q000201:enzymology; D008847:Micromonospora / Q000254:growth & development*; D010456:Peptides, Cyclic / Q000302:isolation & purification / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000494:pharmacology; D011817:Rabbits
D000806:Angiotensin-Converting Enzyme Inhibitors; D010456:Peptides, Cyclic; D011480:Protease Inhibitors; C052543:K-13 (ACE inhib)