The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates
The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates
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DOI：
10.1016/j.bmcl.2007.03.060
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发表时间：
2007-06-01
影响因子：
2.7
通讯作者：
Boddy, Christopher N.
中科院分区：
文献类型：
--
作者：
Sharma, Krishna K.;Boddy, Christopher N.
来自匹马菌素和6-脱氧阿糖胞苷B生物合成途径的重组聚酮合酶硫酯酶结构域催化许多简单的N-乙酰基半胱胺硫酯衍生物的水解。这项研究表明，硫酯酶是不是高度底物选择性的酰基酶中间体的形成，在非核糖体肽合酶硫酯酶结构域，显示出非常高的特异性底物加载相反。这一观察结果对生物合成工程具有重要意义;生产聚酮化合物产品的途径。(C)2007爱思唯尔有限公司版权所有。
The recombinant polyketide synthase thioesterase domains from the pimaricin and 6-deoxyerythronolide B biosynthetic pathways catalyze hydrolysis of a number of simple N-acetylcysteamine thioester derivatives. This study demonstrates that thioesterases are not highly substrate selective in formation of the acyl-enzyme intermediate, in contrast to non-ribosomal peptide synthase thioesterase domains that show very high specificity for substrate loading. This observation has important implications for the engineering of biosynthetic; pathways to produce polyketide products. (C) 2007 Elsevier Ltd. All rights reserved.