• Phosphorylation
  • Glycolysis Step 2 Voet, Voet & Pratt 20012 Fig. 15.3 Phosphorylation of Fructose 6-P G= -14.2 kJ/mol Glycolysis Step 3 Berg, Tymoczko & Stryer, 2012 Chap 16 Stage 2 of Glycolysis Berg, Tymoczko & Stryer, 2002 chap 16. (slidegur.com)
  • The liver isoform is regulated by phosphorylation of a serine residue at the NH 2 terminus (Ser-32) by cAMP-dependent protein kinase, which leads to an increase in the bisphosphatase-to-kinase activity ratio. (physiology.org)
  • amino acids stimulate Fru-2,6-P2 synthesis by Akt-dependent PFKFB2 phosphorylation and activation and show how signaling and metabolism are inextricably linked. (nih.gov)
  • Enzyme
  • the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK2) catalyzes both the formation of fructose-2,6-bisphosphate (fructose-2,6-P 2 ) and its degradation ( 26 , 27 , 35 ). (physiology.org)
  • 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. (nih.gov)
  • protein
  • Binding of glucokinase to glucokinase regulatory protein is counteracted by fructose-1-phosphate, and accordingly precursors of fructose-1-phosphate cause translocation of glucokinase from the nucleus to the cytoplasm ( 2 , 33 ). (physiology.org)
  • This PFK2 variant, when expressed at high levels, reverses the inhibitory effects of glucagon on glycolysis, fructose-2,6-P 2 , and glucokinase translocation, indicating a role for either PFK2 protein or its product fructose-2,6-P 2 in mediating the effects of glucagon. (physiology.org)
  • increase
  • A persistent increase in 6-phosphofructo-2-kinase produced by a change in PFK-2/FBPase-2 isoform expression that may play an important role in the regulation of muscle glycolysis. (nih.gov)
  • glucose
  • 2. The attachment of the phosphoryl group renders glucose a less stable molecule and more amenable to further metabolic action. (slidegur.com)
  • liver
  • bifunctionality of PFK-2/FBPase-2 complements the metabolic zonation of the liver by ensuring coherent switching in response to insulin and glucagon. (nih.gov)
  • levels
  • However, combined overexpression of glucokinase and PFK2 had a synergistic effect on fructose-2,6-P 2 levels, suggesting that interaction of these enzymes may be a prerequisite for formation of fructose-2,6-P 2 . (physiology.org)