| Literature DB >> 12014445 |
Yasuaki Esumi1, Yoshikatsu Suzuki, Yumiko Itoh, Masakazu Uramoto, Ken-ichi Kimura, Masaaki Goto, Makoto Yoshihama, Teruo Ichikawa.
Abstract
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 beta-carboxyl group of Asp9 and the a-amino group of Gly1.Entities:
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Year: 2002 PMID: 12014445 DOI: 10.7164/antibiotics.55.296
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649