Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051128 | FEBS Letters | 2005 | 6 Pages |
Abstract
The β-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 β-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.
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Plant Science
Authors
Judith Fliegmann, Emilie Montel, Alma Djulić, Sylvain Cottaz, Hugues Driguez, Jürgen Ebel,