摘要

A NMR method related to 2D CH correlation with an additional double quantum filter for P-31 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 beta-anomer of glucose is phosphorylated faster by a factor of 1.4 versus the alpha-anomer. Use of human liver glucokinase as an enzyme yields more complex kinetics.

  • 出版日期2013-5-15

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