Esumi Yasuaki, Suzuki Yoshikatsu, Itoh Yumiko, Uramoto Masakazu, Kimura Ken-ichi, Goto Masaaki, Yoshihama Makoto, Ichikawa Teruo
RIKEN (The Institute of Physical and Chemical Research), Saitama, Japan.
J Antibiot (Tokyo). 2002 Mar;55(3):296-300. 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 beta-carboxyl group of Asp9 and the a-amino group of Gly1.
从微小双孢菌SNA - 115中分离得到的脯氨酰内肽酶新抑制剂前肽素的结构已被确定。快原子轰击质谱法（FAB/MS）、埃德曼降解法和氨基酸分析表明，前肽素是一种由19种常见L - 氨基酸组成的环肽。通过快原子轰击质谱法和蛋白质化学方法，确定前肽素的一级结构为Gly1 - Tyr - Pro - Trp - Trp - Asp - Tyr - Arg - Asp9 - Leu - Phe - Gly - Gly - His - Thr - Phe - Ile - Ser - Pro19，它在Asp9的β - 羧基和Gly1的α - 氨基之间环化。
