Structure-based rational design of a phosphotriesterase

Colin J. Jackson; Kahli Weir; Anthony Herlt; Jeevan Khurana; Tara D. Sutherland; Irene Horne; Christopher Easton; Robyn J. Russell; Colin Scott; John G. Oakeshott

doi:10.1128/AEM.00629-09

Structure-based rational design of a phosphotriesterase

Colin J. Jackson, Kahli Weir, Anthony Herlt, Jeevan Khurana, Tara D. Sutherland, Irene Horne, Christopher Easton, Robyn J. Russell, Colin Scott^*, John G. Oakeshott

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

37 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	5153-5156
Number of pages	4
Journal	Applied and Environmental Microbiology
Volume	75
Issue number	15
DOIs	https://doi.org/10.1128/AEM.00629-09
Publication status	Published - Aug 2009

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title = "Structure-based rational design of a phosphotriesterase",

abstract = "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.",

author = "Jackson, \{Colin J.\} and Kahli Weir and Anthony Herlt and Jeevan Khurana and Sutherland, \{Tara D.\} and Irene Horne and Christopher Easton and Russell, \{Robyn J.\} and Colin Scott and Oakeshott, \{John G.\}",

year = "2009",

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language = "English",

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T1 - Structure-based rational design of a phosphotriesterase

AU - Jackson, Colin J.

AU - Weir, Kahli

AU - Herlt, Anthony

AU - Khurana, Jeevan

AU - Sutherland, Tara D.

AU - Horne, Irene

AU - Easton, Christopher

AU - Russell, Robyn J.

AU - Scott, Colin

AU - Oakeshott, John G.

PY - 2009/8

Y1 - 2009/8

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/67651252932

U2 - 10.1128/AEM.00629-09

DO - 10.1128/AEM.00629-09

M3 - Article

SN - 0099-2240

VL - 75

SP - 5153

EP - 5156

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

IS - 15

ER -

Structure-based rational design of a phosphotriesterase

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