Structure-Based Rational Design of a Phosphotriesterase

被引：31

作者：

Jackson, Colin J. ^{[1
]}

Weir, Kahli ^{[1
]}

Herlt, Anthony ^{[2
]}

Khurana, Jeevan ^{[1
]}

Sutherland, Tara D. ^{[1
]}

Horne, Irene ^{[1
]}

Easton, Christopher ^{[2
]}

Russell, Robyn J. ^{[1
]}

Scott, Colin ^{[1
]}

Oakeshott, John G. ^{[1
]}

机构：

[1] CSIRO Entomol, Canberra, ACT 2601, Australia

[2] Australian Natl Univ, Res Sch Chem, Acton, ACT 0200, Australia

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2009年 / 75卷 / 15期

关键词：

ORGANOPHOSPHORUS HYDROLASE; BACTERIAL PHOSPHOTRIESTERASE; SUBSTRATE; SPECIFICITY; HYDROLYSIS;

D O I：

10.1128/AEM.00629-09

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In silico substrate docking of both stereoisomers of the pesticide chlorfenvinphos (CVP) in the phosphotriesterase from Agrobacterium radiobacter identified two residues (F131 and W132) that prevent productive substrate binding and cause stereospecificity. A variant (W131H/F132A) was designed that exhibited ca. 480-fold and 8-fold increases in the rate of Z-CVP and E-CVP hydrolysis, respectively, eliminating stereospecificity.

引用

页码：5153 / 5156

页数：4

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