Collection of Czechoslovak Chemical Communications - digital archive 

Abstract

N-Maleyl-L-amino acid and peptide esters were synthesized and employed as substrates for α-chymotrypsin. From the k_cat/K_M values can be suggested that benzyl esters are significantly better substrates than the appropriate methyl esters. Further improvement in the substrate properties results from the introduction of the p-nitrobenzyl ester moiety. The choline ester of benzyloxycarbonyl-L-phenylalanine with the highest k_cat/K_M value confirmed the P₁' leaving group specificity for positively charged residues. From the kinetic data can be concluded that acyl donors with high k_cat/K_M values, which are useful in kinetically controlled enzymatic peptide synthesis, need not contain aromatic amino acid residues in the P₁ position.