K-4, a novel inhibitor of angiotensin I converting enzyme produced by Actinomadura spiculosospora.
- 1 January 1986
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 39 (3), 364-371
- https://doi.org/10.7164/antibiotics.39.364
Abstract
A novel inhibitor of angiotensin I converting enzyme (ACE), named K-4, was isolated from the culture broth of Actinomadura spiculosospora nov. sp. K-4. The K-4 was an oligopeptide containing L-phenylalanine with (R)-1-amino-2-(4-hydroxyphenyl)ethylphosphonic acid as the C-terminal residue. The compound proved to be a specific and reversible inhibitor of ACE with the inhibition constant (Ki) of 0.18 .mu.M, and inhibited ACE non-competitively by use of hippuryl-L-histidyl-L-leucine (HHL) as a substrate. When administrated intravenously to rats, K-4 inhibited the pressor response to angiotensin I.This publication has 6 references indexed in Scilit:
- K-26, a novel inhibitor of angiotensin I converting enzyme produced by an Actinomycete K-26.The Journal of Antibiotics, 1986
- Isolation and characterization of I5B2, a new phosphorus containing inhibitor of angiotensin I converting enzyme produced by Actinomadura sp.The Journal of Antibiotics, 1984
- Design of Specific Inhibitors of Angiotensin-Converting Enzyme: New Class of Orally Active Antihypertensive AgentsScience, 1977
- PORCINE PANCREATIC CARBOXYPEPTIDASE A SYSTEM .1. 3 FORMS OF ACTIVE ENZYME1963
- CARBOXYPEPTIDASE-B .4. PURIFICATION AND CHARACTERIZATION OF THE PORCINE ENZYME1960
- A MODIFIED SPECTROPHOTOMETRIC DETERMINATION OF CHYMOTRYPSIN, TRYPSIN, AND THROMBINCanadian Journal of Biochemistry and Physiology, 1959