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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.

SUBMITTER: Jackson CJ

PROVIDER: S-EPMC2725513 | biostudies-other | 2009 Aug

REPOSITORIES: biostudies-other

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Structure-based rational design of a phosphotriesterase.

Jackson Colin J CJ Weir Kahli K Herlt Anthony A Khurana Jeevan J Sutherland Tara D TD Horne Irene I Easton Christopher C Russell Robyn J RJ Scott Colin C Oakeshott John G JG

Applied and environmental microbiology 20090605 15

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. ...[more]

PMID: 19502439

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