Studies on the hydrolytic properties of (serine) carboxypeptidase Y.

摘要: The activity of serine carboxypeptidases is dependent on a catalytic triad, an oxyanion hole, and binding site equivalent to those found in the endopeptidases. action carboxypeptidase Y substrates containing amino acids, alcohols, amines as leaving groups described. It demonstrated that features common endopeptidases are sufficient for hydrolysis ester bonds. However, rapid amide bonds interactions between C-terminal carboxylate group substrate recognition enzyme. Furthermore, basis pH dependencies wild-type mutant enzyme, combined with ability enzyme utilize energy promote catalysis, alternative models high at low discussed. They describe how catalytically essential histidine maintained its active deprotonated state through perturbation pKa value enzyme-substrate complex.