K-13, a novel inhibitor of angiotensin I converting enzyme produced by Micromonospora halophytica subsp. exilisia. I Fermentation, isolation and biological properties.

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Abstract
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 .mu.M. K-13 hardly inhibited carboxypeptidase A, trypsin, .alpha.-chymotrypsin, leucine aminopeptidase, and aminopeptidase B even at a level of 61 .mu.M. When K-13 was administered intravenously to rats, it inhibited the pressor response to angiotensin I.

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