差向异构结构域在非核糖体肽合成中的作用  

The role of epimerization domain in the synthesis of nonribosomal peptides

作　　者：薛永常[1] 吴欣园 朱晨阳 Xue Yongchang;Wu Xinyuan;Zhu Chenyang(School of Biological Engineering,Dalian Polytechnic University,Dalian 116034)

机构地区：[1]大连工业大学生物工程学院,大连116034

出　　处：《中国抗生素杂志》2023年第8期841-846,共6页Chinese Journal of Antibiotics

基　　金：辽宁省自然科学基金项目(No.20180550858);辽宁省教育厅高校基本科研项目(No.LJKMZ20220899)。

摘　　要：差向异构结构域作为非核糖体肽合成酶体系中重要组分,将L型氨基酸异构化为D型氨基酸,赋予了非核糖体肽独特的生物活性和对蛋白酶的抵抗力。本文结合近期研究阐述了差向异构结构域的蛋白结构特征和异构化过程中的去质子化/再质子化机制,此外还对差向异构结构域在非核糖肽合成中的调控作用进行了总结,展望了非核糖体肽合成酶的未来发展趋势,希望为非核糖体肽合成酶的工程改造和新药的研发提供理论基础和依据。As an important component in the system of nonribosomal peptide synthetase,the epimerization domain isomerizes L-amino acids into D-amino acids,giving nonribosomal peptides unique biological activity and resistance to protease.Combined with recent research,this paper describes the protein structural characteristics of the epimerization domain and the mechanism of deprotonation/re-protonation during isomerization.In addition,the regulatory role of epimerization domains in nonribosomal peptide synthesis is summarized,and the future development trend of nonribosomal peptide synthase is prospected,in order to provide a theoretical basis for the engineering modification of nonribosomal peptide synthase and development of new medicines.

关 键 词：非核糖体肽合成酶 差向异构结构域 非核糖体肽 立体化学转化 构象 

分 类 号：Q71[生物学—分子生物学]