6. Phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate tofructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzymeis a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulatedby phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucotiol-1,6-diphosphate.(a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function ofsubstrate concentration to show a sigmoidal or hyperbolic curve in the absence of any regulators?(b) How would each of the regulators above affect the dynamics of the T state to R state equilibriumof phosphofructokinase? Briefly explain your reasoning.(c) If it were possible to isolate phosphofructokinase monomers in an active form, how would youexpect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP,AMP, and 2,5-anhydro-D-glucotiol-1,6-diphosphate? Explain your answers.

Name: 6. Phosphofructokinase is an allosteric enzyme that catalyzes the con
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Description: 6. Phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate tofructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzymeis a homotetramer that is inhibited by ATP bindi

In mammals, the allosteric regulation of phosphofructokinase is primarily achieved through the…

Answered: 6. Phosphofructokinase is an allosteric…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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6. Phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to
fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme
is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated
by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucotiol-1,6-diphosphate.
(a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of
substrate concentration to show a sigmoidal or hyperbolic curve in the absence of any regulators?
(b) How would each of the regulators above affect the dynamics of the T state to R state equilibrium
of phosphofructokinase? Briefly explain your reasoning.
(c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you
expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP,
AMP, and 2,5-anhydro-D-glucotiol-1,6-diphosphate? Explain your answers.

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For B in the answer it is mentioned,

"If the allosteric regulators increased the affinity of the enzyme for its substrates, then the equilibrium would shift to the right, and more of the enzyme would be in the R state. If the allosteric regulators decreased the affinity of the enzyme for its substrates, then the equilibrium would shift to the left, and more of the enzyme would be in the T-state."

I don't know how this answers the question though in regards to how the enzyme is affected by its regulators as mentioned in at the top of the problem with ATP, AMP, Phosphorylation and 2,5-anhydro-D-Glucotiol-1,6-diphosphate. Could this answer be restated or reexplained?

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I'm a bit confused for part c answer to this question, would it be possible to restate the answer and explain?

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