Substrate Activation in the Carboxypeptidase A Catalysis of Ester Hydrolysis

  title={Substrate Activation in the Carboxypeptidase A Catalysis of Ester Hydrolysis},
  author={Joe Murphy and John W. Bunting},
  journal={Canadian Journal of Chemistry},
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... 
Influence of the substrate structure on carboxypeptidase Y catalyzed peptide bond formation
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.
Chapter 4 Carboxypeptidase A
pH dependence of the hydrolysis of hippuric acid esters by carboxypeptidase A.
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.