ABSTRACT
The rational application of proteases in preparative peptide synthesis requires an insight into specificity and efficiency of these enzymes as catalysts for peptide bond formation. A systematic study on the kinetics of thermolysin-catalyzed peptide bond formation was reported by Wayne and Fruton. The kinetic data obtained strongly emphasized the influence of the P2'-site of the amine components on chymotryptic peptide synthesis. The specificity of pepsin-controlled peptide syntheses was studied by Bozler et al. by exploring the influence of a series of carboxyl- and amine components on the initial rates of the respective synthetic processes. In addition, pepsin exhibits a preference for hydrophobic residues in the P2-position, and as such a phenylalanine-anilide in the P1-site was superior to a leucine anilide in this position. The molecular mechanism of a-chymotryptic and ß-tryptic peptide bond formation has been studied by Riechmann and Kasche.
