phosphofructokinase deficiency
enfermedad de Tarui
phosphofructokinase oor Spaans
phosphofructokinase
en
(biochemistry) Any of a group of kinase enzymes that convert fructose phosphates to biphosphates
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fosfofructoquinasa
en
enzyme
Fosfofructoquinasa
en
2 versions: pfk-1 (Q427147) and pfk-2 (Q420663)
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Phosphofructokinase
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Fosfofructoquinasa
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voorbeelde
Advanced filtering
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Phosphofructokinase is the most important regulator of glycolysis because it is the rate-limiting step.
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Phosphofructokinase is inhibited more or less completely by physiological concentrations of ATP.
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Regulation of Phosphofructokinase-1 D.
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The regulatory properties of the Escherichia coli phosphofructokinase-1 are described in Section 5.10A.
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Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis.
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A key step for the regulation of glycolysis is an early reaction in the pathway catalysed by phosphofructokinase-1 (PFK1).
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Fructose 2,6-bisphosphate is formed by phosphorylation of fructose 6-phosphate by phosphofructokinase-2.
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A model of one of the four identical subunits of phosphofructokinase.
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The absence of the M isoenzyme of phosphofructokinase can also be demonstrated in blood cells and fibroblasts.
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Fructose catabolism bypasses phosphofructokinase-1 and its associated regulation.
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Phosphofructokinase-1 is allosterically inhibited by ATP and allosterically activated by AMP.
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Protein kinase A catalyzes the phosphorylation of phosphofructokinase-2 (Section 11.5C).
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Phosphofructokinase catalyzes the phosphorylation of fructose 6-phosphate.
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Fructose 2,6-bisphosphate is formed by phosphorylation of fructose 6-phosphate by phosphofructokinase-2.
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Glycogen synthase and phosphofructokinase are inhibited by phosphorylation and thus are stimulated by insulin.
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Elevated expression of Fru-2,6-P2 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.
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It relieves inhibition of phosphofructokinase-1 by ATP and increases the affinity for fructose 6-phosphate.
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Among several molecular mechanisms by which the increase in free fatty acids could raise insulin resistance is decrease in xylulose-5-phosphate that leads to an inhibition of phosphofructokinase-2, and consequently to a blockade in glycol sis with a subsequent increase in the final products of the hexosamine pathway and activation of PKC has been proposed as well as known activator of IKKB that inhibits tyrosine phosphorilation of IRS, hindering glucose transport.
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This regulates the reaction catalyzing fructose-2,6-bisphosphate (a potent activator of phosphofructokinase-1, the enzyme that is the primary regulatory step of glycolysis) by slowing the rate of its formation, thereby inhibiting the flux of the glycolysis pathway and allowing gluconeogenesis to predominate.
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Evidence for inhibition of glycolysis in the parasite at the phosphofructokinase reaction8 has been found.
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These irreversible glycolytic reactions are catalyzed by pyruvate kinase, phosphofructokinase-1, and hexokinase.
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Glucagon inhibits several key steps in glycolysis, including phosphofructokinase and pyruvate kinase.
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The steps catalyzed by hexokinase, phosphofructokinase-1, and pyruvate kinase are metabolically irreversible. 5.
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Further production of phosphoenolpyruvate is prevented by inhibiting phosphofructokinase-1.
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For example, many of the properties of phosphofructokinase-1 from E. coli fit the concerted theory.
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