The hydrolysis of esters of N-hippurylglycine and N-pivaloylglycine by carboxypeptidase A.

@article{Bunting1978TheHO,
  title={The hydrolysis of esters of N-hippurylglycine and N-pivaloylglycine by carboxypeptidase A.},
  author={John W. Bunting and Samuel S.-T. Chu},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={524 2},
  pages={
          393-402
        }
}
The kinetics of the hydrolysis of five esters of N-hippurylglycine (C6H5CONHCH2CONHCH2CO2CRR1CO2H (2 approximately) and seven esters of N-pivaloylglycine ((CH3)3CCONHCH2CRR1CO2H (3 approximately)) by bovine pancreatic carboxypeptidase A (Peptidyl-L-amino-acidhydrolase, EC 3.4.12.2) have been studied at pH 7.5, 25 degrees C and ionic strength 0.5. All N-hippurylglycine esters (2: R=H, R1=H, C2H5, 4-ClC6H4, C6H5CH2) display Michaelis-Menten kinetics up to at least 0.1 M substrate. The N… 
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Data is available which can only be interpreted in terms of at least three enzymic sites being available for hydrophobic interactions with ester substrate molecules.
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Reversible inhibition of the hydrolysis of O-hippuryl-L-3-phenyllactic acid by carboxypeptidase A has been studied for a series of decarboxylic acids at 25°, pH 7.5, and ionic strength 0.2. All
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