This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Horne, I.
Right arrow Articles by Oakeshott, J. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Horne, I.
Right arrow Articles by Oakeshott, J. G.
Agricola
Right arrow Articles by Horne, I.
Right arrow Articles by Oakeshott, J. G.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, July 2002, p. 3371-3376, Vol. 68, No. 7
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.7.3371-3376.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification of an opd (Organophosphate Degradation) Gene in an Agrobacterium Isolate

Irene Horne,* Tara D. Sutherland, Rebecca L. Harcourt,,{dagger} Robyn J. Russell, and John G. Oakeshott

CSIRO Entomology, Canberra, ACT 2601, Australia

Received 12 December 2001/ Accepted 4 April 2002

We isolated a bacterial strain, Agrobacterium radiobacter P230, which can hydrolyze a wide range of organophosphate (OP) insecticides. A gene encoding a protein involved in OP hydrolysis was cloned from A. radiobacter P230 and sequenced. This gene (called opdA) had sequence similarity to opd, a gene previously shown to encode an OP-hydrolyzing enzyme in Flavobacterium sp. strain ATCC 27551 and Brevundimonas diminuta MG. Insertional mutation of the opdA gene produced a strain lacking the ability to hydrolyze OPs, suggesting that this is the only gene encoding an OP-hydrolyzing enzyme in A. radiobacter P230. The OPH and OpdA proteins, encoded by opd and opdA, respectively, were overexpressed and purified as maltose-binding proteins, and the maltose-binding protein moiety was cleaved and removed. Neither protein was able to hydrolyze the aliphatic OP malathion. The kinetics of the two proteins for diethyl OPs were comparable. For dimethyl OPs, OpdA had a higher kcat than OPH. It was also capable of hydrolyzing the dimethyl OPs phosmet and fenthion, which were not hydrolyzed at detectable levels by OPH.

* Corresponding author. Mailing address: CSIRO Entomology, GPO Box 1700, Canberra, ACT 2601, Australia. Phone: 61 2 6246 4110. Fax: 61 2 6246 4173. E-mail: irene.horne{at}ento.csiro.au.

{dagger} Present address: Proteome Systems Ltd., North Ryde, NSW 1670, Australia.

Applied and Environmental Microbiology, July 2002, p. 3371-3376, Vol. 68, No. 7
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.7.3371-3376.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gorla, P., Pandey, J. P., Parthasarathy, S., Merrick, M., Siddavattam, D. (2009). Organophosphate Hydrolase in Brevundimonas diminuta Is Targeted to the Periplasmic Face of the Inner Membrane by the Twin Arginine Translocation Pathway. J. Bacteriol. 191: 6292-6299 [Abstract] [Full Text]  
  • Jackson, C. J., Weir, K., Herlt, A., Khurana, J., Sutherland, T. D., Horne, I., Easton, C., Russell, R. J., Scott, C., Oakeshott, J. G. (2009). Structure-Based Rational Design of a Phosphotriesterase. Appl. Environ. Microbiol. 75: 5153-5156 [Abstract] [Full Text]  
  • Jiang, H., Yang, C., Qu, H., Liu, Z., Fu, Q. S., Qiao, C. (2007). Cloning of a Novel Aldo-Keto Reductase Gene from Klebsiella sp. Strain F51-1-2 and Its Functional Expression in Escherichia coli. Appl. Environ. Microbiol. 73: 4959-4965 [Abstract] [Full Text]  
  • Mee-Hie Cho, C., Mulchandani, A., Chen, W. (2006). Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides. Protein Eng Des Sel 19: 99-105 [Abstract] [Full Text]  
  • Singh, B. K., Walker, A., Morgan, J. A. W., Wright, D. J. (2004). Biodegradation of Chlorpyrifos by Enterobacter Strain B-14 and Its Use in Bioremediation of Contaminated Soils. Appl. Environ. Microbiol. 70: 4855-4863 [Abstract] [Full Text]  
  • McLoughlin, S. Y., Jackson, C., Liu, J.-W., Ollis, D. L. (2004). Growth of Escherichia coli Coexpressing Phosphotriesterase and Glycerophosphodiester Phosphodiesterase, Using Paraoxon as the Sole Phosphorus Source. Appl. Environ. Microbiol. 70: 404-412 [Abstract] [Full Text]  
  • Singh, B. K., Walker, A., Morgan, J. A. W., Wright, D. J. (2003). Effects of Soil pH on the Biodegradation of Chlorpyrifos and Isolation of a Chlorpyrifos-Degrading Bacterium. Appl. Environ. Microbiol. 69: 5198-5206 [Abstract] [Full Text]  
  • Siddavattam, D., Khajamohiddin, S., Manavathi, B., Pakala, S. B., Merrick, M. (2003). Transposon-Like Organization of the Plasmid-Borne Organophosphate Degradation (opd) Gene Cluster Found in Flavobacterium sp.. Appl. Environ. Microbiol. 69: 2533-2539 [Abstract] [Full Text]  
  • Yang, H., Carr, P.D., McLoughlin, S.Y., Liu, J.W., Horne, I., Qiu, X., Jeffries, C.M.J., Russell, R.J., Oakeshott, J.G., Ollis, D.L. (2003). Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution. Protein Eng Des Sel 16: 135-145 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»