Peptidases definition

Serine and cysteine peptidases are not perfect acyltransferases. Therefore, it is useful to have a method for the prediction of the outcome of the kinetically controlled peptide synthesis. In order to get a simple efficiency parameter we decided to introduce the partition value p11061 analogous with the definition of the Michaelis constant according to Eq. (3), where P2 = Ac-OH, P3 = Ac-N, and N = HN. 

An understanding of the molecular interactions between the acylenzyme and the attacking nucleophilic amine component allows an optimization of the acyl transfer efficiency. The efficiency of the nucleophilic attack of the amine component depends essentially on an optimal binding within the active site by S - P interactions (Fig. 12.5-11). Consequently, more information on the specificity of the S subsites of serine and cysteine peptidases are useful, which can be obtained by systematic acyl transfer studies using libraries of nucleophilic amine components. According to the definition of the p value (see above) small values of p indicate high S subsite specificity for the appropriate amine component in peptidase-catalyzed acyl transfer reactions. 

The definition of the scope of the specificity of proteolytic enzymes with regard to the chemical configurations in the vicinity of the hydrolyzable peptide bond has necessarily been restricted to their peptidase activity in order that substrates of known chemical structure can be used. The familiar classification of proteinases on the basis of specificity towards peptides as model substrates, ss, 84, 85 meet rigorous testing on those rare... 

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