Structure-Based Rational Design of a Phosphotriesterase | Zendy

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

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Structure-Based Rational Design of a Phosphotriesterase

Author(s) -

Colin J. Jackson,

Kahli M. Weir,

Anthony J. Herlt,

Jeevan L. Khurana,

Tara D. Sutherland,

Irene Horne,

Christopher J. Easton,

Robyn J. Russell,

Colin Scott,

John G. Oakeshott

Publication year - 2009

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.00629-09

Subject(s) - stereospecificity , in silico , hydrolysis , chemistry , substrate (aquarium) , docking (animal) , stereochemistry , enzyme , biochemistry , biology , catalysis , ecology , gene , medicine , nursing

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.

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