非核糖体肽合成酶硫酯酶结构域研究进展

The research progress of thioesterase domain in non-ribosomal peptide synthetase

微生物可通过非核糖体肽合成酶(nonribosomal peptide synthetases,NRPS)催化合成众多结构和功能多样的次级代谢产物——非核糖体肽(nonribosomal peptide,NRP)。NRPS装配线由多个模块组成,其中末端硫酯酶(thioesterase,TE)结构域由于其独特的水解和环化双重活性,对于产物释放及线性多肽的体外环化具有重要意义。本文主要对TE催化的产物释放机制以及其非常规的功能方面进行综述,为研发新的NRPs类化合物以及环肽的体外合成提供理论依据。

Microorganisms can catalyze the synthesis of numerous nonribosomal peptides(NRPs)of secondary metabolites with diverse structures and functions through nonribosomal peptide synthetase(NRPS).The NRPS assembly line consists of several modules.Because of its unique hydrolysis and cyclization activity,the terminal thioesterase(TE)domain is of great significance for product release and in vitro cyclization of linear peptides.This paper mainly reviews the product release mechanism and its unconventional functions catalyzed by TE,in order to provide a theoretical basis for the development of new NRPs compounds and the synthesis of cyclic peptides in vitro.