A NMR method to determine the anomeric specificity of glucose phosphorylation

A NMR method related to 2D CH correlation with an additional double quantum filter for 31P spin coupling was employed to follow the reaction kinetics of the two anomers of glucose during phosphorylation catalyzed by the enzyme yeast hexokinase. The kinetic parameters according to Michaelis–Menten for these reactions have been determined and it is shown that the β-anomer of glucose is phosphorylated faster by a factor of 1.4 versus the α-anomer. Use of human liver glucokinase as an enzyme yields more complex kinetics.

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