Abstract
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.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
