Reversible Inhibition of Carboxypeptidase A. IV. Inhibition of Specific Esterase Activity by Hippuric Acid and Related Species and other Amino Acid Derivatives and a Comparison with Substrate Inhibition

@article{Bunting1975ReversibleIO,
  title={Reversible Inhibition of Carboxypeptidase A. IV. Inhibition of Specific Esterase Activity by Hippuric Acid and Related Species and other Amino Acid Derivatives and a Comparison with Substrate Inhibition},
  author={John W. Bunting and Chester D. Myers},
  journal={Canadian Journal of Chemistry},
  year={1975},
  volume={53},
  pages={1993-2004}
}
The anions of each of the following carboxylic acids exhibit uncompetitive inhibition of the hydrolysis of O-hippuryl-L-3-phenyllactic acid by bovine carboxypeptidase A at pH 7.5, 25°, ionic streng... 
View via Publisher
11 Citations

11 Citations

Citation Type

Citation Type

Synergistic inhibition of carboxypeptidase A by zinc ion and imidazole.
  • W. L. Mock, L. Wang
  • Chemistry, Biology
    Biochemical and biophysical research communications
  • 1999
Zinc ion in solution yields a 560-fold enhancement in the kinetic inhibition of carboxypeptidase A by the simple heterocycle imidazole, behavior attributed to formation of a ternary complex of the…
Substrate inhibition in the hydrolysis of N-acylglycine esters by carboxypeptidase A.
The pH dependence of peptide hydrolysis by nitrocarboxypeptidase A.
The pH-dependence of the non-specific esterase activity of carboxypeptidase A.
pH dependence of the hydrolysis of hippuric acid esters by carboxypeptidase A.
TLDR
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.
The hydrolysis of esters of N-hippurylglycine and N-pivaloylglycine by carboxypeptidase A.
Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution.
Calculation of the free energy of association for protein complexes
  • N. Horton, M. Lewis
  • Chemistry
    Protein science : a publication of the Protein Society
  • 1992
TLDR
A method for calculating the association energy of quaternary complexes starting from their atomic coordinates is developed and it is shown that the calculated association can be used as a predictive tool for analyzing modeled molecular complexes.
Prediction of binding constants of protein ligands: A fast method for the prioritization of hits obtained from de novo design or 3D database search programs
  • H. Böhm
  • Chemistry, Biology
    J. Comput. Aided Mol. Des.
  • 1998
TLDR
A new empirical scoring function is presented that estimates the free energy of binding for a protein–ligand complex of known 3D structure and is suitable for the application in a 3D database search or de novo ligand design program such as LUDI.
The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
  • H. Böhm
  • Chemistry, Biology
    J. Comput. Aided Mol. Des.
  • 1994
SummaryA new simple empirical function has been developed that estimates the free energy of binding for a given protein-ligand complex of known 3D structure. The function takes into account hydrogen…
...
1
2
...