Abstract
Oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous α-amylase catalyzed by horseradish peroxidase results in the loss of the inhibitory activity against both enzymes. The enzymatic oxidation is accompanied by modification of one methionine and two tryptophan residues in the protein. The results obtained, together with data on chemical modification and limited proteolysis, allow us to conclude that Met 34-Ala 35 is the reactive site of the inhibitor responsible for the interaction with subtilisin. It is supposed that the reactive site of the inhibitor responsible for the interaction with α-amylase contains one or two tryptophan residues.
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