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Enzymatic oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous α‐amylase
Author(s) -
Gvozdeva Ekaterina L.,
Valueva Tatyana A.,
Mosolov Vladimir V.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81683-q
Subject(s) - subtilisin , chemistry , proteolysis , biochemistry , bifunctional , enzyme , tryptophan , horseradish peroxidase , amino acid , catalysis
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.