水分子在A类β -内酰胺酶酰基化结构的去酰化中的作用。

Drug design and discovery Pub Date : 1999-08-01
M Ishiguro, S Imajo
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引用次数: 0

摘要

青霉素和戊烯酮酰化酶的分子动力学模拟表明,结合间隙中酰基部分的构象灵活性和酰基部分的构象变化对去酰化至关重要。Glu 166残基附近的水分子不是去酰化的亲核试剂,但氧阴离子四面体中间体模型的构建表明,水分子可能是氧阴离子促进去酰化的质子供体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The role of water molecules in the deacylation of acylated structures of class A beta-lactamase.

Molecular dynamics simulation of the penicillin- and penem-acylated enzymes reveals that the conformational flexibility of the acyl moieties in the binding cleft and the conformational change of the acyl moieties are crucial for deacylation. The water molecule adjacent to the Glu 166 residue is not the nucleophile for deacylation, but construction of a model of the oxyanion tetrahedral intermediate suggested a plausible role of the water molecule as a proton donor for the oxyanion to facilitate the deacylation.

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