Stereochemical constraints on the substrate specificity of phosphotriesterase.

@article{Hong1999StereochemicalCO,
  title={Stereochemical constraints on the substrate specificity of phosphotriesterase.},
  author={Sungmin Hong and Frank M Raushel},
  journal={Biochemistry},
  year={1999},
  volume={38 4},
  pages={
          1159-65
        }
}
A series of achiral, chiral, and racemic mixtures of paraoxon analogues containing various combinations of methyl, ethyl, isopropyl, or phenyl substituents were synthesized as probes of the stereochemical constraints within the active site of phosphotriesterase. The kinetic constants for these paraoxon analogues with the enzyme varied significantly with the size of substituents surrounding the phosphorus center. These results indicate that binding and catalysis depend significantly on the… CONTINUE READING

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Purification of Laboratory Chemicals

  • G. A. Omburo, J. M. Kuo, L. S. Mullins, F. M. Raushel
  • Enzymes
  • 1992

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