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Applied and Environmental Microbiology, August 2009, p. 5153-5156, Vol. 75, No. 15
0099-2240/09/$08.00+0     doi:10.1128/AEM.00629-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Structure-Based Rational Design of a Phosphotriesterase{triangledown} ,{dagger}

Colin J. Jackson,1,{ddagger} Kahli Weir,1,{ddagger} Anthony Herlt,2 Jeevan Khurana,1 Tara D. Sutherland,1 Irene Horne,1 Christopher Easton,2 Robyn J. Russell,1 Colin Scott,1* and John G. Oakeshott1

CSIRO Entomology, GPO Box 1700, Canberra, Australian Capital Territory 2601, Australia,1 Research School of Chemistry, Australian National University, Acton, Australian Capital Territory 0200, Australia2

Received 18 March 2009/ Accepted 30 May 2009

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.

* Corresponding author. Mailing address: CSIRO Entomology, GPO Box 1700, Canberra, ACT 2601, Australia. Phone: 61 2 6246 4090. Fax: 61 2 6246 4173. E-mail: colin.scott{at}csiro.au

{triangledown} Published ahead of print on 5 June 2009.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

{ddagger} Contributed equally to this work.

Applied and Environmental Microbiology, August 2009, p. 5153-5156, Vol. 75, No. 15
0099-2240/09/$08.00+0     doi:10.1128/AEM.00629-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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