The inhibition pattern of bovine kidney γ-glutamyl transpeptidase by maleic acid was analysed for the inference of the nature of acceptor binding site of the enzyme. Since the inhibition of the enzyme by maleic acid occured only in the presence of ac...
The inhibition pattern of bovine kidney γ-glutamyl transpeptidase by maleic acid was analysed for the inference of the nature of acceptor binding site of the enzyme. Since the inhibition of the enzyme by maleic acid occured only in the presence of acceptor molecules, it was likely that maleic acids bind on acceptor binding site. And the transpeptidation was predominant at high substrate concentration, whereas the hydrolysis was predominant at low substrate concentration. The optimum pH of the enzyme was shifted to lower pH with the concentr??tion decrease. These results imply that the exposure of certain functional groups of acceptor binding site on the enzyme is regulated according to physiological conditions. On the other hands, the suggestion that the presence of a common binding site for donor and acceptor should be reconsidered because the substrate inhibition did not occur at high concentration of glycylglycine.