Enantiomeric specificity at the deacylation process of tryptic catalysis.

Trypsin-specific substrate analogs, 'inverse substrates', carrying chiral acyl group were synthesized. Kinetic analysis of the trypsin-catalyzed hydrolysis of these substrates revealed that the deacylation process is also appropriate for discrimination between enantiomers. The enantiomeric preference during the deacylation process was analyzed by comparing the hydrolytic rates corresponding to eight enantiomeric pairs of the substrates. The spatial requirement of the enzyme active site for catalytic efficiency is discussed, based on the steric characteristics of the optically active acyl residues.