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通过对过渡态进行设计的长程静电稳定作用提高猪胰磷脂酶A2的活性。

Increased activity of porcine pancreatic phospholipase A2 by designed long-range electrostatic stabilisation of the transition state.

作者信息

Sheffield P J, Bhat K M, Owen A J, Perry B, Sumner I G, Warwicker J

机构信息

Institute of Food Research, Reading Laboratory, UK.

出版信息

Biochem Biophys Res Commun. 1995 Nov 22;216(3):778-84. doi: 10.1006/bbrc.1995.2689.

DOI:10.1006/bbrc.1995.2689
PMID:7488193
Abstract

Stabilisation of the catalytic transition state by long-range charge interactions has been tested with mutagenesis for porcine pancreatic phospholipase A2. Electrostatics calculations were used to determine locations which would interact preferentially with one part of the dipolar charge separation that is believed to develop in the transition state. Experiment shows increased enzyme activity relative to wild-type recombinant enzyme for mutants N97D and N101D, consistent with the design.

摘要

通过诱变对猪胰磷脂酶A2进行了长程电荷相互作用稳定催化过渡态的测试。静电计算用于确定那些优先与过渡态中可能形成的偶极电荷分离的一部分相互作用的位置。实验表明，与野生型重组酶相比，突变体N97D和N101D的酶活性增加，与设计相符。

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