Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase.

@article{Pinot1995MolecularAB,
  title={Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase.},
  author={Franck Pinot and David F. Grant and Jeffrey K. Beetham and Antony Parker and Babak Borhan and Solveig Landt and A. Daniel Jones and Bruce D Hammock},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 14},
  pages={7968-74}
}
In order to investigate the involvement of amino acids in the catalytic mechanism of the soluble epoxide hydrolase, different mutants of the murine enzyme were produced using the baculovirus expression system. Our results are consistent with the involvement of Asp-333 and His-523 in a catalytic mechanism similar to that of other alpha/beta hydrolase fold enzymes. Mutation of His-263 to asparagine led to the loss of approximately half the specific activity compared to wild-type enzyme. When His… CONTINUE READING
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