Kinetics of the reaction catalyzed by Bacillus stearothermophilus glucokinase using the carboxy-terminated PAMAM-bound adenine nucleotides as cofactors

摘要

The initial rates of the reaction catalyzed by Bacillus stearothermophilus glucokinase(GK)were measured using a new family of polymer-bound adenosine S'-triphosphate(ATP)as a cofactor.The initial reaction rates measured under wide cofactor concentration conditions were correlated well with the rate equation which was derived previously based on the reaction rates measured using native ATP.However,the kinetic parameters were considerably different from those determined using the data obtained using native ATP.