Catalysis by dienelactone hydrolase: a variation on the protease mechanism.

@article{Cheah1993CatalysisBD,
  title={Catalysis by dienelactone hydrolase: a variation on the protease mechanism.},
  author={Elizabeth S T Cheah and Gary W. Ashley and J. Gary and David L. Ollis},
  journal={Proteins},
  year={1993},
  volume={16 1},
  pages={64-78}
}
Dienelactone hydrolase (DLH), an enzyme from the beta-ketoadipate pathway, catalyzes the hydrolysis of dienelactone to maleylacetate. Our inhibitor binding studies suggest that its substrate, dienelactone, is held in the active site by hydrophobic interactions around the lactone ring and by the ion pairs between its carboxylate and Arg-81 and Arg-206. Like the cysteine/serine proteases, DLH has a catalytic triad (Cys-123, His-202, Asp-171) and its mechanism probably involves the formation of… CONTINUE READING

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