Steps in the reactions of chymotrypsin with tyrosine derivatives

Publisher Website
Google Scholar
Abstract
The reactions between chymotrypsin and the p-nitrophenyl ester of N-benzyloxy-carbonyl L-tyrosine have been studied by a fast-reaction photometric method. It has been shown that an N-benzyloxycarbonyl-L-tyrosine-chymotrypsin compound is formed as an intermediate in the enzymic hydrolysis of this substrate. The formation of this intermediate compound is so fast (k>lOOO sec.-1) that its kinetics could not be studied. A comparison of the reaction parameters of the chymotrypsin-catalyzed hydrolysis of the amide, ethyl ester and p-nitrophenyl ester of tyrosine gives further support to a 3-step reaction scheme for enzymic hydrolysis, which has been previously proposed.

This publication has 5 references indexed in Scilit: