Reprogramming Promiscuous Nonribosomal Peptide Synthetases for Production of Specific Peptides,Organic Letters

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Reprogramming Promiscuous Nonribosomal Peptide Synthetases for Production of Specific Peptides
Organic Letters ( IF 4.9 ) Pub Date : 2019-03-12 00:00:00 , DOI: 10.1021/acs.orglett.9b00395
Xiaofeng Cai _{1,

2} , Lei Zhao ₁ , Helge B. Bode _{1,

3}

Affiliation

Pairs of docking domains (DDs) mediate the selective interations between adjacent nonribosomal peptide synthetases (NRPSs) to form defined protein–protein interactions resulting in defined peptide sequences. New specific rhabdopeptide/xenortide-like peptides (RXPs) were generated by swapping of either flexible or nonfunctional DD pairs between these monomodular RXP-NRPSs against DDs from collinear NRPSs. The results presented a promising means of engineering RXP-producing NRPSs to obtain desired peptides and further substantiated the decisive role of DDs in the NRP synthesis.

中文翻译：

重新编程混杂的非核糖体肽合成酶以生产特定的肽

成对的对接结构域（DDs）介导相邻的非核糖体肽合成酶（NRPSs）之间的选择性相互作用，形成确定的蛋白-蛋白相互作用，从而产生确定的肽序列。通过将这些单模块RXP-NRPS之间的柔性或非功能性DD对与共线NRPS的DD交换，可以生成新的特定的rhabdopeptide / xenortide-like肽（RXP）。结果提供了一种有希望的方法，可工程化生产RXP的NRPS，以获得所需的肽，并进一步证实了DD在NRP合成中的决定性作用。

更新日期：2019-03-12

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