Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

@article{Blow1969RoleOA,
  title={Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin},
  author={David M. Blow and Jens J. Birktoft and Brian S. Hartley},
  journal={Nature},
  year={1969},
  volume={221},
  pages={337-340}
}
The catalytic site of chymotrypsin contains an interior aspartic acid hydrogen-bonded to a histidine which in its turn is hydrogen-bonded to a serine. Polarization of the system due to the buried negative charge of the aspartic acid residue would make the serine oxygen strongly nucleophilic and would explain its reactivity towards amides and esters. 

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