· Fructose 2,6-bisphosphate activates by decreasing KF-6-P by about 15-fold and has an activation constant of 92 nM, while AMP decreases KF-6-P about 6-fold and has an activation constant of 93 microM. Double activation experiments suggest that fructose 2,6-bisphosphate and AMP are synergistic in their activation.
Selective depletion of fructose 2,6-bisphosphate inhibits glucose-induced recruitment of ChREBP to the G6pc promoter and also induction of G6pc by xylitol and gluconeogenic precursors. The requirement for fructose 2,6-bisphosphate for ChREBP recruitment to the promoter does not exclude the involvement of additional metabolites acting either co-ordinately or at downstream sites.
Fructose 2,6-bisphosphate activates pyrophosphate: fructose-6-phos phate 1-phosphotransferase and increases triose phosphate to hexose phosphate cycling in heterotrophic cells Alisdair R. Fernie*, Albrecht Roscher, R. George Ratcliffe, Nicholas J. Kruger Department of Plant Sciences, University of Oxford, Oxford, OX1 3RB, UK
Since fructose 2,6-bisphosphate is an activator of the glycolytic phosphofructokinase (sometimes called phosphofructokinase-1 for clarity) as well as an inhibitor of fructose 1,6-bisphosphatase, glucagon can thus reduce glycolytic flux and promote gluconeogenesis at this step as well as at the pyruvate kinase step, in addition to its effect of stimulating glycogen breakdown and inhibiting glycogen synthesis.
Fructose 2,6-bisphosphate activates pyrophosphate: fructose-6-phosphate 1-phosphotransferase and increases triose phosphate to hexose phosphate cycling in heterotrophic cells. Abstract: The aim of this work was to establish the influence of fructose 2,6-bisphosphate (Fru-2,6-P2) on non-photosynthetic carbohydrate metabolism in plants.