Mechanisms for activation and inhibition of carboxypeptidase A catalyzed hydrolyses of peptides and esters.
3,3-Diphenylpropanoate (DPP) activates the carboxypeptidase A catalyzed hydrolysis of benzoylglycyl-L-phenylalanine (BzGly-L-Phe) (Ka = 2.1 x 10 (-3) M) and inhibits ester hydrolysis uncompetitively (K1 =2.1 X 10 (-3) M). A common modifier binding site located adjacent to the peptide and ester substrate binding sites is proposed. The forms of the pathways proposed for activation and inhibition are remarkably similar.
D000495:Allosteric Site; D001665:Binding Sites; D002268:Carboxypeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D004952:Esters; D007700:Kinetics; D008433:Mathematics; D010455:Peptides; D010666:Phenylpropionates; D011485:Protein Binding; D013379:Substrate Specificity
D004952:Esters; D010455:Peptides; D010666:Phenylpropionates; C017258:3,3-diphenylpropanoate; D002268:Carboxypeptidases