Characterization of the subsite structure of the beta-glucosidase from Aspergillus niger, an aspect of the mechanism of carbohydrate recognition.
Steady-state kinetics on the reaction catalyzed by the beta-glucosidase of Aspergillus niger were carried out to evaluate the kinetic parameters, Km and ko, for phenyl beta-D-glucosides. The ko/Km values, which may relate to productive binding at subsites, were found to correlate with the substituent constant pi (hydrophobicity), suggesting that subsite 2 has a hydrophobic character. A "hydrophobic-driven" mechanism is considered to contribute to the productive E-S complex for recognition of the substrate.
Department of Biological Function Science, Graduate School of Agriculture, Prefecture University of Kyoto, Japan.
M
M
Ohnishi
G
G
Okada
T
T
Yazaki
D001234:Aspergillus niger / Q000201:enzymology*; D001665:Binding Sites; D005960:Glucosides / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000378:metabolism*
D005960:Glucosides; D001617:beta-Glucosidase