摘要
The crude enzyme (PH-1) isolated from Pseudostellaria heterophylla by ourgroup has catalyzed enzymatic cyclization of linear peptideNH_2-Gly^1-Gly^2-Leu-Pro-Pro-Pro-lle-Phe-COOH (4) into cyclopeptide heterophyllin B (HB) from plantfor the first time. To ensure this reaction, some analytical methods including TLC, HPLC, MS, NMR,and ^(13)C labeling were used to prove that the reaction of substrate 4 sharing residue ofNH-Phe-Gly-CO was successful.
The crude enzyme (PH-1) isolated from Pseudostellaria heterophylla by our group has catalyzed enzymatic cyclization of linear peptide NH2-Gly1-Gly2-Leu-Pro-Pro-Pro-Ile-Phe-COOH (4) into cyclopeptide heterophyllin B (HB) from plant for the first time. To ensure this reaction, some ana-lytical methods including TLC, HPLC, MS, NMR, and 13C labeling were used to prove that the reaction of substrate 4 sharing residue of NH-Phe-Gly-CO was successful.
作者
JIA Aiqun1, LI Xiang2, TAN Ninghua1, LIU Xiaozhu3, SHEN Yuemao1 & ZHOU Jun1 1. State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Graduate Univer-sity of Chinese Academy of Sciences, Chinese Academy of Sciences, Kunming 650204, China
2. Chinese Peptide Co., Ltd, Hangzhou 310018, China
3. Southwest Forestry College, Kunming 650204, China
