The Studies on the Action of Yeast Hexokinaseupon the α- and β-Diasteromers of D-Glucose

Abstract

(1) The velocity of the phosphorylation of α-D-glucose, catalyzed by the purified yeast hexokinase, seems to be greater than that of β-D-glucose. The relative rate of phosphorylation of β-D-glucose is observed to be 60-70 (α-D-glucose=100).
(2) The average Michaelis constants of yeast hexokinase are found to be 1.8×10^-4 and 2.4×10^-4 when it acted on α-D-glucose and β-D-glucose respectively.