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Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution

Yang, H., Carr, P.D., McLoughlin, S.Yu, Liu, J.W., Horne, I., Qiu, X., Jeffries, C.M.J., Russell, R.J., Oakeshott, J.G., Ollis, D.L.·2003·Protein Engineering, Design and Selection

Abstract

Organophosphate-degrading enzyme from Agrobacterium radiobacter P230 (OPDA) is a recently discovered enzyme that degrades a broad range of organophosphates. It is very similar to OPH first isolated from Pseudomonas diminuta MG. Despite a high level of sequence identity, OPH and OPDA exhibit different substrate specificities. We report here the structure of OPDA and identify regions of the protein that are likely to give it a preference for substrates that have shorter alkyl substituents. Directed evolution was used to evolve a series of OPH mutants that had activities similar to those of OPDA. Mutants were selected for on the basis of their ability to degrade a number of substrates. The mutations tended to cluster in particular regions of the protein and in most cases, these regions were where OPH and OPDA had significant differences in their sequences.

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Metadata

Authors
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.
Venue
Protein Engineering, Design and Selection
Published
2003-02
Volume
16
Issue
2
Pages
135-145
ISSN
  • 0269-2139 (ISSN-L)
  • 1741-0134
  • 1741-0126
OpenAlex
W2102825845
Cited by
162
References
0
FWCI
3.11
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution. https://app.cochat.ai/papers/10.1093/proeng/gzg013
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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 Engineering, Design and Selection. https://doi.org/10.1093/proeng/gzg013

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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