The anomeric form of D-fructose 1,6-bisphosphate 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 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.
D006597:Fructose-Bisphosphatase / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005636:Fructosephosphates / Q000378:metabolism*; D007553:Isotope Labeling; D007700:Kinetics; D008968:Molecular Conformation; D009132:Muscles / Q000201:enzymology; D010761:Phosphorus Radioisotopes; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D005636:Fructosephosphates; D010761:Phosphorus Radioisotopes; D006597:Fructose-Bisphosphatase; D005634:Fructose-Bisphosphate Aldolase