Inhibition of Proteolytic Enzymes by Decarboxylated Amino-Acid Derivatives. Effect of Toluenesulphonyl(Tosyl)agmatine (4-Toluenesulphonamidobutylguanidine) on Thrombin and Trypsin

Abstract

PROTEOLYTIC enzymes are known to catalyse the hydrolysis of specific amino-acid esters and amides¹. Specificity is usually determined by the side-chain of the amino-acid contributing the carbonyl function to the bond being split, and, for several reasons, it may be inferred that this ester or amide bond lends very little to the initial binding of the substrate to the enzyme. Thus we suggest that derivatives of specific decarboxylated amino-acids would act as good competitive inhibitors of these enzymes. Since these derivatives would not be subjected to simultaneous hydrolysis, the effect would be longer lasting than that obtained with competing substrates.