SUBSTRATE INHIBITION IN THE HYDROLYSIS OF HIPPURIC ACID ESTERS BY CARBOXYPEPTIDASE A

@article{Murphy1975SUBSTRATEII,
  title={SUBSTRATE INHIBITION IN THE HYDROLYSIS OF HIPPURIC ACID ESTERS BY CARBOXYPEPTIDASE A},
  author={Joe Murphy and John W. Bunting},
  journal={ChemInform},
  year={1975},
  volume={6},
  pages={283-294}
}
The dependence of initial velocity upon substrate concentration has been examined in the carboxypeptidase A catalyzed hydrolysis of the following hippuric acid esters (at pH 7.5, 25°, ionic strength O.5): C6H5CONHCH2CO2CHRCO2H: R=CH3; CH2CH3;(CH2)2CH3; (CH2)3CH3; (CH2)5CH3; CH(CH3)2; CH2CH(CH3)2; C6H5; CH2C6H5. All of these esters display marked substrate inhibition of their enzymic hydrolyses. With the exception of R=CH3, the velocity-substrate concentration profiles for each of these esters… 
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