Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta.

@article{Donarski1989StructureactivityRI,
  title={Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta.},
  author={William J. Donarski and David P. Dumas and D P Heitmeyer and V E Lewis and Frank M Raushel},
  journal={Biochemistry},
  year={1989},
  volume={28 11},
  pages={4650-5}
}
The mechanism and substrate specificity of the phosphotriesterase from Pseudomonas diminuta have been examined. The enzyme hydrolyzes a large number of phosphotriester substrates in addition to paraoxon (diethyl p-nitrophenyl phosphate) and its thiophosphate analogue, parathion. The two ethyl groups in paraoxon can be changed to propyl and butyl groups, but the maximal velocity and Km values decrease substantially. The enzyme will not hydrolyze phosphomonoesters or -diesters. There is a linear… CONTINUE READING
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