Gvozdeva E L, Valueva T A, Mosolov V V
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
FEBS Lett. 1993 Nov 8;334(1):72-4. doi: 10.1016/0014-5793(93)81683-q.
Oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous alpha-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 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-amylase contains one or two tryptophan residues.
辣根过氧化物酶催化的枯草杆菌蛋白酶和内源性α-淀粉酶的双功能小麦抑制剂的氧化作用导致对这两种酶的抑制活性丧失。酶促氧化伴随着蛋白质中一个甲硫氨酸和两个色氨酸残基的修饰。所获得的结果，连同化学修饰和有限蛋白酶解的数据，使我们能够得出结论，Met34-Ala35是抑制剂与枯草杆菌蛋白酶相互作用的反应位点。据推测，抑制剂与α-淀粉酶相互作用的反应位点含有一个或两个色氨酸残基。
