Reversible Dissociation of Glycolytic Enzymes: Kinetic Studies on Lactate Dehydrogenase, Glyceraldehyde 3-Phosphate Dehydrogenase and Aldolase

e.g. phosphoglucomutase, glucose 6-phosphate dehydrogenase and fructose 6-phosphate kinase. However, if the reaction occurs distant from the anomeric carbon atom of the substrate the enzymes show no anomeric specificity, e.g. hexokinase, glucokinase and glucose 6-phosphatase (Wurster & Hess, 1974~). A search for enzymes catalysing anomerization reactions leads to the following conclusion. For D-glucose, D-glucose 6-phosphate and D-fructose 6-phosphate, anomerization reactions catalysed by aldose 1-epimerase (D-glucose, and at acid pH also D-glucose 6-phosphate: Gernert & Keston, 1974), by glucose 6-phosphate 1-epimerase (D-glucose 6-phosphate) and glucose phosphate isomerase (D-glucose 6-phosphate and D-fructose 6-phosphate) occur (Wurster & Hess, 1974~). At the level of D-glucose 6-phosphate, where a-D-glucopyranose 6-phosphate is selectively produced in glycogen catabolism in the reaction catalysed by phosphoglucomutase, and where ,/f-D-glucopyranose 6-phosphate is the specific substrate of glucose 6-phosphate dehydrogenase, an enzymecatalysed anomerization reaction seems to be significant with respect to a control of the pentose phosphate pathway versus glycolysis (Wurster & Hess, 19746).