Isolation and characterization of ancovenin, a new inhibitor of angiotensin I converting enzyme, produced by actinomycetes.
Ancovenin, an inhibitor of angiotensin I converting enzyme isolated from the culture broth of a Streptomyces species, is a dialysable peptide composed of sixteen amino acid residues containing unusual amino acids such as threo-beta-methyllanthionine, meso-lanthionine, and dehydroalanine.
D000596:Amino Acids / Q000032:analysis; D000806:Angiotensin-Converting Enzyme Inhibitors; D001430:Bacteriocins; D002851:Chromatography, High Pressure Liquid; D003470:Culture Media; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D010455:Peptides / Q000302:isolation & purification* / Q000494:pharmacology; D010456:Peptides, Cyclic; D013053:Spectrophotometry; D013302:Streptomyces / Q000254:growth & development
D000596:Amino Acids; D000806:Angiotensin-Converting Enzyme Inhibitors; D001430:Bacteriocins; D003470:Culture Media; D010455:Peptides; D010456:Peptides, Cyclic; C039867:ancovenin