Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.

@article{ChenGoodspeed2001EnhancementRA,
  title={Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.},
  author={Misty Chen-Goodspeed and Miguel Angel Sogorb and Fang Wu and Frank M Raushel},
  journal={Biochemistry},
  year={2001},
  volume={40 5},
  pages={1332-9}
}
The factors that govern the substrate reactivity and stereoselectivity of phosphotriesterase (PTE) toward organophosphotriesters containing various combinations of methyl, ethyl, isopropyl, and phenyl substituents at the phosphorus center were determined by systematic alterations in the dimensions of the active site. The wild type PTE prefers the S(P)-enantiomers over the corresponding R(P)-enantiomers by factors ranging from 10 to 90. Enlargement of the small subsite of PTE with the… CONTINUE READING
21 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

References

Publications referenced by this paper.

BI001549D 3 Some of the mutants created for this investigation have been tested as catalysts for the hydrolysis of the military type organophosphonate nerve agents

  • C. S. McDaniel, L. L. Harper, J. R. Wild
  • J. Bacteriol
  • 1988

Similar Papers

Loading similar papers…