Abstract
Because of the complexity involved in binding of a ligand to an enzyme the conformational preference of the bound ligand has not been well understood yet. We have examined the conformational energies of ligands for carboxypeptidase A using ab initio calculations. Considering the large stereoelectronic effect of 4-5 kcal/mol, the energetic preference of the unbound ligand conformers which arises from the stereoelectronic effect appears to play a significant role in determining the bound ligand conformations.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
3-Mercaptopropionic Acid / analogs & derivatives
-
3-Mercaptopropionic Acid / chemistry
-
3-Mercaptopropionic Acid / metabolism
-
Binding Sites
-
Carboxypeptidases / antagonists & inhibitors
-
Carboxypeptidases / chemistry*
-
Carboxypeptidases / metabolism
-
Carboxypeptidases A
-
Dipeptides / chemistry
-
Dipeptides / metabolism
-
Lactates / chemistry
-
Lactates / metabolism
-
Ligands*
-
Molecular Structure
-
Phenylalanine / analogs & derivatives
-
Phenylalanine / chemistry
-
Phenylalanine / metabolism
-
Phenylpropionates / chemistry
-
Phenylpropionates / metabolism
-
Substrate Specificity
Substances
-
Dipeptides
-
Lactates
-
Ligands
-
Phenylpropionates
-
Phenylalanine
-
2-benzyl-3-mercaptopropanoic acid
-
glycyltyrosine
-
3-Mercaptopropionic Acid
-
Carboxypeptidases
-
Carboxypeptidases A
-
N-acetylphenylalanine