The influence of structure on the hydrolysis of substituted phenyl α-d-glucosides by α-glucosidase

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Abstract
The hydrolysis by [alpha]-glucosidase of phenyl [alpha]-D-glucoside and nine of its substitution products has been studied; the equilibrium constants for the formation of the enzyme-substrate complexes and the first-order velocity constants for their decomposition have been evaluated. A new method for assessing the significance of experimentally determined enzyme-substrate equilibrium constants is proposed. The equilibrium constants have been correlated with the electronic properties of the substituents, as measured by their substituent constants, and a mechanism for the com-bination of [alpha]-glucosidase with aryl [alpha]-D-glucosides is suggested. No similar correlation of the velocity constants with structure was possible.