Add time:07/28/2019         Source:sciencedirect.com

A series of amino, amidino, and aminomethyl derivatives of benzene and cyclohexane were investigated for their inhibitory effect on the activation of trypsinogen. In agreement with earlier reports, amidines were generally much more potent than amines. p-Amidinophenylpyruvic acid, a newly synthesized compound, was found to be the strongest small-molecular inhibitor known so far, surpassing even p-aminobenzamidine. The Ki value of this compound was determined as 9.6 × 10−7m for the enterokinase-catalyzed activation of trypsinogen and as 2.6 × 10−6m for the autocatalytic activation. p-Amidinophenylpyruvic acid was also the most effective inhibitor of tryptic caseinolysis, though the inhibitor constant of 1.2 × 10−4m was considerably greater than the value for the autocatalytic activation.The compounds behaved as noncompetitive inhibitors of the two activation processes as well as of the caseinolytic reaction. This observation is in contrast to the competitive nature of the inhibitory effect when esters or amides are employed as substrates for trypsin. The difference is probably explained by the importance of the specificity site of the active center as a binding site for synthetic substrates while proteins may be able to attach themselves to the enzyme independently from the specificity site.

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