Determine the effect each given mutation would have on the rate of glycolysis in muscle cells.

a. loss of binding site for fructose 1 ,6-bisphophate in pyruvate kinase.
b. loss of allosteric binding site for ATP in pyruvate kinase.
c. loss of allosteric binding site for AMP in phosphofructokinase.
d. loss of regulatory binding site for ATP in phosphofructokinase.

1. Increase
2. decrease
3. No effect

Answer:

a. Decrease

b. Increase

c. Increase

d. No effect

Explanation:

Glycolysis is present in muscle cells which converts glucose to pyruvate, water and NADH. It produces two molecules of ATP. Cellular respiration produces more molecules of ATP from pyruvate in mitochondria. Glycolysis increases in pyruvate kinase.

a. Loss of binding site for fructose 1,6-bisphosphate in pyruvate kinase: Decrease

b. Loss of allosteric binding site for ATP in pyruvate kinase: No effect

c. Loss of allosteric binding site for AMP in phosphofructokinase: Increase

d. Loss of regulatory binding site for ATP in phosphofructokinase: Increase

A. An important substrate in the glycolysis pathway is fructose 1,6-bisphosphate. It stimulates pyruvate kinase, an essential enzyme in glycolysis. The amount of pyruvate kinase that is activated will decrease if the fructose 1,6-bisphosphate binding site in pyruvate kinase is eliminated. As a result the rate of glycolysis in the muscle cells will probably decrease.

B. The allosteric ATP binding site of pyruvate kinase controls how active the enzyme is. However, pyruvate kinase is not significantly regulated by ATP in muscle cells. Therefore, it is unlikely that deletion of the ATP-binding allosteric site in pyruvate kinase would have no effect on the rate of glycolysis in muscle cells.

C. The rate-limiting enzyme in glycolysis, phosphofructokinase, is activated from all forms by AMP. It increases the rate of glycolysis by stimulating the activity of phosphofructokinase. If the allosteric binding site for AMP is eliminated, phosphofructokinase activation will be reduced. As a result, the rate of glycolysis in muscle cells will decrease.

D. Phosphofructokinase is inhibited allosterically by ATP. It regulates the rate of glycolysis by a feedback mechanism. High ATP concentrations cause phosphofructokinase to bind to its regulatory site, limiting its activity and delaying glycolysis. If the regulatory binding site for ATP is eliminated, the inhibitory action of ATP on phosphofructokinase would be lost. As a result, muscle cells will glycolysis at a faster rate.

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