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Pyruvate kinase is subject to allosteric regulation. i) Describe the metabolic importance of regulating flux through...

Pyruvate kinase is subject to allosteric regulation.
i) Describe the metabolic importance of regulating flux through the pyruvate kinase reaction. [5]
ii) Explain the advantage of activating pyruvate kinase with fructose-1,6-bisphosphate. [5]

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Pyruvate kinase

Pyruvate kinasecatalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding one molecule of pyruvate and one molecule of ATP in the final step of glycolysis.

Metabolic importance of regulating flux through the pyruvate kinase reaction.

The reaction of catalysis by pyruvate kinase is one of the three rate-affecting steps of glycolysis and is a highly energetically favorable and irreversible reaction. This step is highly regulated and is irreversible because pyruvate is a crucial intermediate for further metabolic pathways such as Krebs Cycle under aerobic conditions or Lactic Acid fermentation or alcoholic fermentation in anaerobic condition.

Allosteric regulation

The binding of an effector to a site on the protein other than the active site, causes a conformational change and alters the activity of that given enzyme.

Advantage of activating pyruvate kinase with fructose-1,6-bisphosphate

Pyruvate kinase has been found to be allosterically activated by Fructose-1,6-bisphosphate (FBP) and it is alosterically deactivated by alanine and ATP.

Fructose-1,6-bisphosphate is a glycolytic intermediate produced from the phosphorylation of fructose 6-phosphate in an earlier step in the glycolytic pathway itself. It provides feedforward stimulation as an intermediate present within the glycolytic pathway. Pyruvate kinase is most sensitive to the effects of FBP among its effectors.The higher the concentration of FBP, the greater will be the allosteric activation and hence activity of pyruvate kinase.

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