Abstract
alpha-Chymotrypsin is rapidly and completely inactivated by a series of halomethylated derivatives of dihydrocoumarins at pH 7 and 25 degrees. The inactivation is pH-dependent and optimal at neutral pH; it is also more or less complete depending on the excess of inhibitor with respect to the enzyme. These compounds are substrates for alpha-chymotrypsin and, during the catalytic process, a latent alkylating function of the reagent is activated at the active site of the enzyme and reacts with some vicinal nucleophilic amino acid residues. The stoichiometry of the reaction of the corresponding radioactive reagents with the enzyme is slightly superior to one, but one histidine residue of alpha-chymotropsin is mainly modified. This histidine is identified as histidine-57 by the diagonal peptide mapping method. In comparison with other reagents, the efficiency of these suicide substrates" and particularly that one of a derivative (compound 2) carrying a substrate-like side chain is found to be very high.
Published Version
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