The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases.

@article{Dunn2000TheTS,
  title={The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases.},
  author={Ben Dunn and S Hung},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1477 1-2},
  pages={231-40}
}
Like most proteolytic enzymes, the aspartic proteinases bind substrates and most inhibitors within an extended active site cleft. Bound ligands typically adopt a beta-strand conformation. Interactions with groups on both sides of the cleft determine the primary as well as secondary specificity of the enzymes. We have pursued the discovery of the sometimes subtle distinctions between members of the aspartic proteinase family by two routes. In the first case, we have constructed sets of… CONTINUE READING

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