Pyruvate kinase
Cofactors used
Clinical / pharmacological. PK deficiency: chronic non-spherocytic haemolytic anaemia
What it does, reaction by reaction
Glycolysis Carbohydrate Metabolism · Cytosol
Phosphoenolpyruvate + ADP → pyruvate + ATP
Converts Phosphoenolpyruvate ADP into Pyruvate ATP
› Notes
Pyruvate kinase requires K+ and Mg2+ (or Mn2+) and performs the second substrate-level phosphorylation. This step is irreversible; in liver it is an important regulatory point and is activated feed-forward by fructose-1,6-bisphosphate. It occurs twice per glucose and yields two additional ATP.
Anaerobic Glycolysis / Lactic Acid Fermentation Energy Metabolism & Cellular Respiration · Cytosol
Phosphoenolpyruvate + ADP → pyruvate + ATP
Converts Phosphoenolpyruvate ADP into Pyruvate ATP
› Notes
Required cofactors: ADP, Mg2+, and K+. This is essentially irreversible and a major regulatory step; it is activated feed-forward by fructose-1,6-bisphosphate in many tissues. The second substrate-level phosphorylation generates two ATP per glucose at this stage.
Showing all 2 reactions.
What accelerates and inhibits it
Regulation is pathway-specific, so each context is listed separately
Anaerobic Glycolysis / Lactic Acid Fermentation
Fructose-1,6-bisphosphate; ADP
ATP, alanine; hepatic phosphorylation inhibits the L isoform
Insulin promotes dephosphorylation/activation and expression of liver pyruvate kinase; glucagon/epinephrine phosphorylate and inhibit hepatic pyruvate kinase
Glycolysis
Listed there as: Pyruvate kinase (liver isoform)
Fructose-1,6-bisphosphate
ATP, alanine; phosphorylation
Insulin promotes dephosphorylation and activity; glucagon/epinephrine activate protein kinase A, phosphorylating and inhibiting the liver isoform
Recent literature
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