摘要
聚酮合成酶能够合成包括许多大环内酯类抗生素在内的聚酮类天然产物,它的结构和功能的模块性为组合生物合成的产生和发展奠定了基础。聚酮合成酶的酰基转移酶功能域可以特异性地决定所选择酰基辅酶A的种类,决定产物的结构。近年来,针对许多来源不同、结构各异的聚酮合成酶的底物专一性已经从氨基酸序列、结构和功能等方面进行了大量的研究,为更有效地应用聚酮合成酶开发新型抗生素奠定了基础。
Polyketide synthases catalyze the synthesis of complex natural products including macrolide antibiotics from simple precursors such as propionyl-CoA and methylmalonyl-CoA. The structural and functional modularity of these multienzyme systems has raised the possibility that polyketide biosynthetic pathways might be rationally reprogrammed by combinatorial manipulation. Previous studies have shown that the choice of these substrates is primarily controlled by individual acyltransferase （AT） domains within each PKS and the intracellular acyl-CoA pools. An essential prerequisite for harnessing this biosynthetic potential is a better understanding of the molecular recognition features of polyketide synthases. Within this decade, a variety of genetic, biochemical, and chemical investigations have yielded insights into the specificity of several architecturally different polyketide synthases. The results of these studies, together with their implications for biosynthetic engineering, are summarized in this review.
出处
《中国抗生素杂志》
CAS
CSCD
北大核心
2006年第11期641-645,664,共6页
Chinese Journal of Antibiotics
基金
国家自然科学基金资助(30570042)
关键词
聚酮合成酶
底物专一性
组合生物合成
酰基转移酶
Polyketide synthase
Substrate specificity
Combinatorial biosynthesis
Acyltransferase
作者简介
朱峰，女，生于1981年，硕士研究生。研究方向为抗生索发酵。;通讯作者:乔建军，E-mailtjianjunq@du．edu．Cn
