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Fru-2,6-P 2 strongly activates glucose breakdown in glycolysis through allosteric modulation (activation) of phosphofructokinase 1 (PFK-1).Elevated expression of Fru-2,6-P 2 levels in the liver allosterically activates phosphofructokinase 1 by increasing the enzyme’s affinity for fructose 6-phosphate, while decreasing its affinity for inhibitory ATP and citrate.
Phosphofructokinase-2 (6-phosphofructo-2-kinase, PFK-2) or fructose bisphosphatase-2 (FBPase-2), is an enzyme indirectly responsible for regulating the rates of glycolysis and gluconeogenesis in cells. It catalyzes formation and degradation of a significant allosteric regulator, fructose-2,6-bisphosphate (Fru-2,6-P 2) from substrate fructose-6 ...
The enzyme fructose-2,6-bisphosphate 2-phosphatase ({EC 3.1.3.46) catalyzes the reaction . β-D-fructose 2,6-bisphosphate + H 2 O D-fructose 6-phosphate + phosphateThis enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds.
Function [ edit ] The bifunctional 6-phosphofructo-2-kinase ( EC 2.7.1.105 )/fructose-2,6-bisphosphatase ( EC 3.1.3.46 ) (PFKFB) regulates the steady-state concentration of fructose 2,6-bisphosphate , an activator of a key regulatory enzyme of glycolysis , phosphofructokinase .
This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. Two transcript variants encoding two different isoforms have been found for this gene. [5]
The TP53-inducible glycolysis and apoptosis regulator (TIGAR) also known as fructose-2,6-bisphosphatase TIGAR is an enzyme that in humans is encoded by the C12orf5 gene. [ 5 ] [ 6 ] [ 7 ] TIGAR is a recently discovered enzyme that primarily functions as a regulator of glucose breakdown in human cells .
Researcher found that iPFK2 has a beta-hairpin N-terminal structure that secures the binding of fructose-6-phosphate to the active site via interaction with the protein's ‘2-Pase’ domain. There are two active pockets within iPFK2 for fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase which are structurally different.
Fructose-2,6-bisphosphate (F2,6P 2) also stimulates GK transcription, it seems by way of Akt2 rather than SREBP1c. It is not known whether this effect is one of the downstream effects of activation of insulin receptors or independent of insulin action. Levels of F2,6P 2 play other amplifying roles in glycolysis in hepatocytes.