Catalytic properties of the bifunctional soybean beta-glucan-binding protein, a member of family 81 glycoside hydrolases.
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.
Fliegmann
Judith
J
Department Biologie I - Botanik, LMU, Menzinger Str. 67, D-80638 München, Germany. fliegmann@lrz.uni-muenchen.de
Montel
Emilie
E
Djulić
Alma
A
Cottaz
Sylvain
S
Driguez
Hugues
H
Ebel
Jürgen
J
D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D003001:Cloning, Molecular; D005936:Glucans / Q000378:metabolism; D006026:Glycoside Hydrolases; D006868:Hydrolysis; D037102:Lectins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010940:Plant Proteins; D013025:Glycine max / Q000737:chemistry*; D013237:Stereoisomerism; D013379:Substrate Specificity
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins; D005936:Glucans; D037102:Lectins; D010940:Plant Proteins; C037937:glucan-binding proteins; D006026:Glycoside Hydrolases