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JBC, Vol. 250, Issue 13, 4883-4887, Jul, 1975

The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions

K. J. Schray, R. Fishbein, W. P. Bullard and S. J. Benkovic

From a series of rapid quench kinetic experiments, it has been demonstrated that muscle D-fructose bisphosphate aldolase catalyzes the cleavage of beta-D-fructose 1,6-bisphosphate but not that of the alpha anomer, although the alpha anomer may be tightly bound. Yeast D-fructose bisphosphate aldolase appears to utilize both alpha and beta anomers of the substrate, with yeast apoaldolase catalyzing the interconversion of the alpha and beta forms.
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