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Ch. 9 - Cellular Respiration and Fermentation
Chapter 9, Problem 8

MAKE CONNECTIONS Step 3 in Figure 9.9 is a major point of regulation of glycolysis. The enzyme phosphofructokinase is allosterically regulated by ATP and related molecules (see Concept 8.5). Considering the overall result of glycolysis, would you expect ATP to inhibit or stimulate activity of this enzyme? Explain. (Hint: Make sure you consider the role of ATP as an allosteric regulator, not as a substrate of the enzyme.)

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Step 1: Understand the role of phosphofructokinase (PFK) in glycolysis. PFK catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate, which is a key regulatory step in glycolysis.
Step 2: Recognize that ATP acts as an allosteric regulator of PFK. Allosteric regulation involves the binding of a molecule at a site other than the enzyme's active site, which affects the enzyme's activity.
Step 3: Consider the overall result of glycolysis, which is the production of ATP. High levels of ATP indicate that the cell has sufficient energy.
Step 4: Analyze the feedback inhibition mechanism. When ATP levels are high, ATP binds to the allosteric site of PFK, inhibiting its activity. This prevents the overproduction of ATP and conserves glucose.
Step 5: Conclude that ATP inhibits the activity of phosphofructokinase. This regulation ensures that glycolysis is slowed down when energy (ATP) is abundant, maintaining energy homeostasis in the cell.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Glycolysis

Glycolysis is a metabolic pathway that converts glucose into pyruvate, producing ATP and NADH in the process. It consists of ten enzyme-catalyzed reactions and is crucial for cellular respiration. The pathway is divided into two phases: the energy investment phase, where ATP is consumed, and the energy payoff phase, where ATP is produced. Understanding glycolysis is essential for grasping how cells generate energy from glucose.
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Allosteric Regulation

Allosteric regulation refers to the modulation of an enzyme's activity through the binding of an effector molecule at a site other than the active site. This binding can either enhance (activator) or inhibit (inhibitor) the enzyme's function. In the case of phosphofructokinase, ATP acts as an allosteric inhibitor, signaling that the cell has sufficient energy, thus slowing down glycolysis when ATP levels are high.
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Phosphofructokinase (PFK)

Phosphofructokinase (PFK) is a key regulatory enzyme in glycolysis that catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. It is considered the 'committed step' of glycolysis, as it determines the pathway's flow towards energy production. PFK is allosterically regulated by ATP and other metabolites, making it a critical control point in cellular metabolism, particularly in response to the energy needs of the cell.
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