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Question: Phosphofructokinase is an enzyme that acts on fructose-6-phosphate at an early step in glucose breakdown. Regulation of this enzyme controls whether the sugar will continue on in the glycolytic pathway. Considering this graph, under which condition is phosphofructokinase more active? Given what you know about glycolysis and regulation of metabolism by this enzyme, explain the mechanism by which phosphofructokinase activity differs depending on ATP concentration. Explain why it makes sense that regulation of this enzyme has evolved so that its works this way.

Short Answer

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Phosphofructokinase (PFK) is more active under low ATP (adenosine triphosphate) concentration. This is because the slope is steeper at lower ATP concentration than the slope at higher ATP concentration.

The activity of PFK increases in the presence of lower ATP concentration. On the other hand, the enzyme is inhibited when the ATP concentration is high in the cell.

The allosteric inhibition of PFK indicates that cells have a high amount of ATP, and glycolysis is not required by the cells of the body.

Step by step solution

01

Glycolysis and role of PFK on glycolysis

The process by which glucose molecule is degraded by the cell to produce energy intermediates such as ATP and NADPH (nicotinamide adenine dinucleotide phosphate) is called glycolysis.Thus, glycolysis is the process by which the body obtains energy from glucose.

In glycolysis, PFK catalyzes the synthesis of fructose-1,6-biphosphate from fructose-6-phosphate.It utilizes ATP for the phosphorylation of fructose-6-phosphate.

02

Explanation for the enzyme to be more active under low ATP concentration

From the graph, it can be inferred that the slope under low ATP concentration is very steep and reaches its peak quickly. On the contrary, the slope at high ATP concentration is not very steep and reaches its peak much laterthan the slope at low ATP concentration.

This exhibits that phosphofructokinase is more active under low ATP concentration as compared to high ATP concentration.

03

Explanation for the PFK activity is dependent on ATP concentration

PFK is a key regulatory enzyme of the glycolysis pathway. Increased levels of ATP concentration allosterically inhibit the enzyme. This means ATP inhibits the affinity of PFK for fructose-6-phosphate. As a result, the activity of PFK decreases in the presence of high ATP concentration.

On the other hand, the enzyme is stimulated at a high AMP (adenosine monophosphate)/ low ATP concentration.This means the low ATP concentration increase the affinity of the enzyme for the substrate.As a result, the activity of the enzyme increases in the presence of low ATP concentration.

04

Step 4: Explanation for the evolution of allosteric inhibition of phosphofructokinase indicates glycolysis is not required

ATP is an allosteric inhibitor for PFK. A high level of ATP indicates that the cell has a high concentration of ATP and, thus, glycolysis that produces energy (ATP) is not required by the cell.Thus, high ATP concentration inhibits the activity of PFK.

On the contrary, a low concentration of ATP indicates that the energy is required by the cell, so glycolysis is stimulated. Thus, low ATP concentration activates the PFK.

Therefore, the allosteric inhibitor of PFK by ATP signals that energy is not required by the cell, thereby inhibiting glycolysis.

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