Propeptin, a New Inhibitor of Prolyl Endopeptidase Produced by Microbispora II. Determination of Chemical Structure

• Published in: Journal of antibiotics Vol. 55; no. 3; pp. 296 - 300
• Main Authors: ESUMI, YASUAKI, SUZUKI, YOSHIKATSU, ITOH, YUMIKO, URAMOTO, MASAKAZU, KIMURA, KEN-ICHI, GOTO, MASAAKI, YOSHIHAMA, MAKOTO, ICHIKAWA, TERUO
• Format: Journal Article
• Language: English
• Published: Tokyo JAPAN ANTIBIOTICS RESEARCH ASSOCIATION 01.03.2002; Japan Antibiotics Research Association
• Subjects: Actinomycetales - metabolism; Amino Acid Sequence; Anti-Bacterial Agents - biosynthesis; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; Antibiotics (antibacterial agents, antifungal agents); Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents; Antibiotics. Antiinfectious agents. Antiparasitic agents; Applied microbiology; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; General aspects; Mass Spectrometry - methods; Medical sciences; Microbiology; Molecular Sequence Data; Peptides, Cyclic - biosynthesis; Peptides, Cyclic - chemistry; Peptides, Cyclic - pharmacology; Pharmacology. Drug treatments; Serine Endopeptidases - metabolism; Serine Proteinase Inhibitors - biosynthesis; Serine Proteinase Inhibitors - chemistry; Serine Proteinase Inhibitors - pharmacology; Microbispora; Serine endopeptidases; Streptosporangiaceae; Enzyme; Prolyl oligopeptidase; Enzyme inhibitor; Fermentation; In vitro; Actinomycetales; Peptidases; Cyclic compound; Polypeptide; Bacteria; Hydrolases; Actinomycetes; Mass spectrometry; Aminoacid sequence; Structural analysis
• ISSN: 0021-8820; 1881-1469
• DOI: 10.7164/antibiotics.55.296

The structure of propeptin, a new inhibitor of prolyl endopeptidase isolated from Microbispora sp. SNA-115, was determined. FAB/MS, Edman degradation and amino acid analysis revealed propeptin to be a cyclic polypeptide consisting of 19 common L-amino acids. By FAB/MS and protein chemical methods, the primary sequence of propeptin was determined to be Gly1-Tyr-Pro-Trp-Trp-Asp-Tyr-Arg-Asp9-Leu-Phe-Gly-Gly-His-Thr-Phe-Ile-Ser-Pro19, which cyclizes between the β-carboxyl group of Asp9 and the α-amino group of Gly1.