剖析模块化聚酮合酶酮还原酶如何与酰基载体蛋白连接的底物相互作用。
Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates.
作者信息
Moretto Luisa, Vance Steven, Heames Brennan, Broadhurst R William
机构信息
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
出版信息
Chem Commun (Camb). 2017 Oct 25;53(83):11457-11460. doi: 10.1039/c7cc04625a. Epub 2017 Oct 5.
Abstract
Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5'-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
摘要
使用从模块化分枝杆菌内酯聚酮合酶切下的片段进行的相互作用研究表明，酮还原酶结构域具有酰基载体蛋白结构域的通用结合位点，并提供了证据表明悬垂的5'-磷酸泛酰巯基乙胺辅基在以正确方向将酰基底物递送至活性位点中起关键作用。
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