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

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