Enzymatic oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous α‐amylase

FEBS Letters

Valueva, Tatyana A.¹  Mosolov, Vladimir V.¹  Gvozdeva, Ekaterina L.¹ 

[1] A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky prospekt 33, 117071 Moscow, Russian Federation

关键词: Enzymatic oxidation;    Bifunctional inhibitor;    Subtilisin;    α-Amylase;   

DOI  :  10.1016/0014-5793(93)81683-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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 α-amylase contains one or two tryptophan residues.

【 授权许可】

Unknown