Pyruvate Kinase: Difference between revisions
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Pyruvate Kinase is the [[Enzyme|enzyme]] that [[Catalysts|catalyses]] the final stage in [[Glycolysis|glycolysis]], changing [[ | Pyruvate Kinase is the [[Enzyme|enzyme]] that [[Catalysts|catalyses]] the final stage in [[Glycolysis|glycolysis]], changing [[Phosphoenolpyruvate|phosphoenolpyruvate]] to [[Pyruvate|pyruvate]], [[Phosphorylation|phosphorylating]] a molecule of [[ADP|ADP]] to [[ATP|ATP]] in the process <ref>Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Company. p456</ref>. | ||
This reaction is irreversible in nature due to the large negative free energy change of -17kJmol<sup>-1<ref>Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Compang. p460</ref></sup>. | This reaction is irreversible in nature due to the large negative free energy change of -17kJmol<sup>-1 <ref>Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Compang. p460</ref></sup>. | ||
[[ATP|ATP]], a product of the reaction, allosterically inhibits the [[Enzyme|enzyme]], as does the [[ | [[ATP|ATP]], a product of the reaction, allosterically inhibits the [[Enzyme|enzyme]], as does the [[Amino acid|amino acid]] [[Alanine|alanine]], slowing the rate of the reaction. The rate of the reaction can be increased by the presence of [[Fructose 1,6-bisphosphate|Fructose 1,6-bisphosphate]], a [[Molecule|molecule]] found in the earlier stages of [[Glycolysis|glycolysis]] <ref>Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Company. p456</ref>. | ||
=== References === | === References === | ||
<references /> | <references /> | ||
Latest revision as of 18:58, 8 January 2011
Pyruvate Kinase is the enzyme that catalyses the final stage in glycolysis, changing phosphoenolpyruvate to pyruvate, phosphorylating a molecule of ADP to ATP in the process [1].
This reaction is irreversible in nature due to the large negative free energy change of -17kJmol-1 [2].
ATP, a product of the reaction, allosterically inhibits the enzyme, as does the amino acid alanine, slowing the rate of the reaction. The rate of the reaction can be increased by the presence of Fructose 1,6-bisphosphate, a molecule found in the earlier stages of glycolysis [3].