title: The control of glycolysis and gluconeogenesis by protein phosphorylation.
abstract: Fructose 2,6-bisphosphate has been discovered as a potent stimulator of liver phosphofructokinase. It is also an inhibitor of fructose 1,6-biphosphatase and a stimulator of PPi: fructose 6-phosphate phosphotransferase from higher plants. It is formed from fructose 6-phosphate and ATP by a 6-phosphofructo 2-kinase and hydrolysed by a fructose 2,6-bisphosphatase. These two enzymes have very similar physicochemical properties and could not be separated from each other. They are substrates for cyclic-AMP-dependent protein kinase, which inactivates the first enzyme and activates the second.
mesh_terms: D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D005635:Fructosediphosphates / Q000037:antagonists & inhibitors / Q000378:metabolism; D005943:Gluconeogenesis; D006019:Glycolysis; D010732:Phosphofructokinase-1 / Q000378:metabolism; D025481:Phosphofructokinase-2; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*
chemical_list: D005635:Fructosediphosphates; C027652:fructose 2,6-diphosphate; D000242:Cyclic AMP; D010770:Phosphotransferases; D011494:Protein Kinases; D025481:Phosphofructokinase-2; D010732:Phosphofructokinase-1; C029063:fructose-1,6-diphosphate