Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.

@article{ChenGoodspeed2001StructuralDO,
  title={Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.},
  author={Misty Chen-Goodspeed and Miguel Angel Sogorb and Fang Wu and Sungmin Hong and Frank M Raushel},
  journal={Biochemistry},
  year={2001},
  volume={40 5},
  pages={1325-31}
}
Bacterial phosphotriesterase (PTE) catalyzes the hydrolysis of a wide variety of organophosphate nerve agents and insecticides. Previous kinetic studies with a series of enantiomeric organophosphate triesters have shown that the wild type PTE generally prefers the S(P)-enantiomer over the corresponding R(P)-enantiomers by factors ranging from 1 to 90. The three-dimensional crystal structure of PTE with a bound substrate analogue has led to the identification of three hydrophobic binding pockets… CONTINUE READING

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