Active-site residue, domain and module swaps in modular polyketide synthases
Active-site residue, domain and module swaps in modular polyketide synthases
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DOI：
10.1007/s10295-003-0062-0
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发表时间：
2003-08-01
影响因子：
3.4
通讯作者：
Leadlay, PF
中科院分区：
文献类型：
--
作者：
Del Vecchio, F;Petkovic, H;Leadlay, PF
来自模块化聚酮合酶 (PKS) 的多个酰基转移酶 (AT) 结构域的序列比较突出了短序列基序与所选延伸单元的性质之间的相关性。当该基序在红糖多孢菌的双模块模型 PKS DEBS1-TE 中被特异性改变时，产物包括三酮内酯，其中在预测位置处掺入了乙酸盐延伸单元而不是丙酸盐单元。我们还描述了一种盒式系统，用于方便地构建基于弗拉迪链霉菌中泰乐菌素 PKS 的混合模块化 PKS，并展示了其在结构域和模块交换中的用途。
Sequence comparisons of multiple acyltransferase (AT) domains from modular polyketide synthases (PKSs) have highlighted a correlation between a short sequence motif and the nature of the extender unit selected. When this motif was specifically altered in the bimodular model PKS DEBS1-TE of Saccharopolyspora erythraea, the products included triketide lactones in which acetate extension units had been incorporated instead of propionate units at the predicted positions. We also describe a cassette system for convenient construction of hybrid modular PKSs based on the tylosin PKS in Streptomyces fradiae and demonstrate its use in domain and module swaps.