ENZYMATIC OXIDATION OF THE BIFUNCTIONAL WHEAT INHIBITOR OF SUBTILISINAND ENDOGENOUS ALPHA-AMYLASE

Oxidation of the bifunctional wheat inhibitor of subtilisin and endoge nous alpha-amylase catalyzed by horseradish peroxidase results in the loss of the inhibitory activity against both enzymes. The enzymatic ox idation is accompanied by modification of one methionine and two trypt ophan residues in the protein. The results obtained, together with dat a on chemical modification and limited proteolysis, allow us to conclu de that Met34-Ala35 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 alpha-amyla se contains one or two tryptophan residues.