Substrate Activation in the Carboxypeptidase A Catalysis of Ester Hydrolysis

@article{Murphy1974SubstrateAI,
  title={Substrate Activation in the Carboxypeptidase A Catalysis of Ester Hydrolysis},
  author={Joe Murphy and John W. Bunting},
  journal={Canadian Journal of Chemistry},
  year={1974},
  volume={52},
  pages={3829-3836}
}
The hydrolyses of the O-hippuryl derivatives of glycolic acid (1a), 2-methyllactic acid (1b), and p-chloromandelic acid (1c) by bovine carboxypeptidase A display substrate activation. The hydrolyse... 
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It is shown that for carboxypeptidase Y catalyzed peptide synthesis the coupling yields are strongly dependent on the C-terminal amino acid residue, indicating the influence of residues other than the one directly involved in acylation of the enzyme.
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The pH dependence (pH 4.5-10.5) of the hydrolysis of seven hippuric acid esters by bovine carboxypeptidase A has been investigated, and the pH dependence of the substrate activation of 1a-c and the substrate inhibition of 1d-g have been compared.
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