Fructose-1,6-bisphosphate is a feedforward allosteric activator of liver pyruvate kinase.
A crucial enzyme in gluconeogenesis is fructose 1,6-bisphosphatase (FBPase). It is a possible target for drugs used to treat type II diabetes. Additionally, the protein is linked to a rare genetic metabolic disorder, and certain cancer cells lack the activity of the enzyme FBPase, which encourages glycolysis and aids in the Warburg effect.
The following reaction is catalyzed by FBPase. The enzyme is controlled allosterically by several small molecules, including AMP and fructose-2,6-phosphate, which are negative regulators, and ATP, which is a positive regulator. Pyruvate kinase activity is activated when FBP attaches to the allosteric binding site on domain C of the enzyme. This conformational shift is brought on by a change in the enzyme's structure.
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