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Catalytic properties of the bifunctional soybean β‐glucan‐binding protein, a member of family 81 glycoside hydrolases
Author(s) -
Fliegmann Judith,
Montel Emilie,
Djulić Alma,
Cottaz Sylvain,
Driguez Hugues,
Ebel Jürgen
Publication year - 2005
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/j.febslet.2005.10.060
Subject(s) - glycoside hydrolase , biochemistry , chemistry , elicitor , cell wall , mode of action , glycine , glucan , stereochemistry , enzyme , amino acid
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.