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  2. Phosphofructokinase 1 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_1

    Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ...

  3. Fructose 2,6-bisphosphate - Wikipedia

    en.wikipedia.org/wiki/Fructose_2,6-bisphosphate

    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.

  4. Enzyme activator - Wikipedia

    en.wikipedia.org/wiki/Enzyme_activator

    It is an isozyme of hexokinase and is found mainly in pancreatic β cells, but also liver, gut, and brain cells where glycolysis cause glucose-induced insulin secretion. [2] Glucokinase activator lowers blood glucose concentrations by enhancing glucose uptake in the liver and increasing insulin production by the pancreatic β cells. [2]

  5. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    F2,6BP is a very potent activator of phosphofructokinase (PFK-1) that is synthesized when F6P is phosphorylated by a second phosphofructokinase . In the liver, when blood sugar is low and glucagon elevates cAMP, PFK2 is phosphorylated by protein kinase A.

  6. Phosphofructokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase

    This protein may use the morpheein model of allosteric regulation. [ 5 ] PFK is about 300 amino acids in length, and structural studies of the bacterial enzyme have shown it comprises two similar (alpha/beta) lobes: one involved in ATP binding and the other housing both the substrate-binding site and the allosteric site (a regulatory binding ...

  7. Glycogenesis - Wikipedia

    en.wikipedia.org/wiki/Glycogenesis

    Returning to glycogen phosphorylase, the less active "b" form can itself be activated without the conformational change. 5'AMP acts as an allosteric activator, whereas ATP is an inhibitor, as already seen with phosphofructokinase control, helping to change the rate of flux in response to energy demand.

  8. PFKL - Wikipedia

    en.wikipedia.org/wiki/PFKL

    6-phosphofructokinase, liver type (PFKL) is an enzyme that in humans is encoded by the PFKL gene on chromosome 21. [5] This gene encodes the liver (L) isoform of phosphofructokinase-1 , an enzyme that catalyzes the conversion of D - fructose 6-phosphate to D - fructose 1,6-bisphosphate , which is a key step in glucose metabolism ( glycolysis ).

  9. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.