Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity.

@article{diSioudi1999ModificationON,
  title={Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity.},
  author={Barbara diSioudi and Janet K. Grimsley and Kai Kien Lai and James R. Wild},
  journal={Biochemistry},
  year={1999},
  volume={38 10},
  pages={
          2866-72
        }
}
  • Barbara diSioudi, Janet K. Grimsley, +1 author James R. Wild
  • Published in Biochemistry 1999
  • Chemistry, Medicine
  • Organophosphorus hydrolase (OPH, EC 8.1.3.1) is a dimeric, bacterial enzyme that detoxifies many organophosphorus neurotoxins by hydrolyzing a variety of phosphonate bonds. The histidinyl residues at amino acid positions 254 and 257 are located near the bimetallic active site present in each monomer. It has been proposed that these residues influence catalysis by interacting with active site residues and the substrate in the binding pocket. We replaced the histidine at position 254 with… CONTINUE READING

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