Catalytic properties of the bifunctional soybean β-glucan-binding protein, a member of family 81 glycoside hydrolases

被引:22
作者
Fliegmann, J
Montel, E
Djulic, A
Cottaz, S
Driguez, H
Ebel, MG
机构
[1] Univ Munich, Dept Biol 1, D-80638 Munich, Germany
[2] CNRS, CERMAV, ICMG, FR 2607, F-38041 Grenoble, France
关键词
plant defence; reaction mechanism; beta-1,3-glucanase; beta-glucan-binding protein; Glycine max;
D O I
10.1016/j.febslet.2005.10.060
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The beta-glucan-binding protein (GBP) of soybean (Glycine max L.) has been shown to contain two different activities. As part of the plasma membrane-localized pathogen receptor complex, it binds a microbial cell wall elicitor, triggering the activation of defence responses. Additionally, the GBP is able to hydrolyze beta-1,3-glucans, as present in the cell walls of potential pathogens. The substrate specificity, the mode of action, and the stereochemistry of the catalysis have been elucidated. This defines for the first time the inverting mode of the catalytic mechanism of glycoside hydrolases belonging to family 81. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:6647 / 6652
页数:6
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