Glucagon stimulates gluconeogenesis in part by decreasing the rate of phosphoenolpyruvate disposal by pyruvate kinase. Changes in PEP binding affinity account for the majority of control of pyruvate kinase activity.
The crucial enzyme known as pyruvate kinase is responsible for the glycolysis cycle's conversion of phosphoenol pyruvate to pyruvate. The ATP molecule is produced in this process.
Allosteric regulation is used to control the pyruvate kinase, and fructose 1,6-bisphosphate activates the enzyme. This regulation is significant because it regulates the metabolites found in various organs. After a specific phase in glycolysis, metabolites from the liver, such as fructose and galactose, enter the process.
In the absence of allosteric activators, the PKM2, PKL, and PKR tetramers demonstrate positive cooperativity of PEP binding.
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