Behavior of trypsin and related enzymes toward amidinophenyl esters.

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Abstract
Kinetics of the hydrolysis of amidinophenyl esters catalyzed by urokinase, kallikrein, plasmin and trypsins from various origins were studied. p-Amidinophenyl esters in which the arrangement of the specific group for bovine trypsin (charged amidinium) is reversed to that of normal substrates were characterized as specific substrates for the enzyme and named inverse substrates. Behavior of these enzymes toward amidinophenyl esters was very similar to that of bovine trypsin. These observations account for the structural similarity of their active sites. p-Amidinophenyl esters were hydrolyzed by clostripain, which is known as a thiol protease with trypsin-like specificity. This is the 1st example of the inverse substrates for a thiol enzyme.