Question

Phosphofructokinase, the major flux-controlling enzyme of glycolysis is allosterically inhibited and activated respectively by
A.ATP and PEP
B. AMP and Pi
C. ATP and ADP
D. Citrate and ATP

Answer 1

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✴️C) ATP and ADP✴️


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Answer 2

Answer:

C. ATP and ADP

Explanation:

Phosphofructokinase (PFK) makes use of ATP to phosphorylate fructose-6-phosphate to fructose-1,6-bisphosphate. As a regulatory enzyme of glycolysis, PFK is negatively inhibited through ATP and citrate and definitely regulated through ADP.

PFK1 is allosterically activated through a excessive attention of AMP, however the maximum effective activator is fructose 2,6-bisphosphate, which is likewise comprised of fructose-6-phosphate through PFK2. Hence, an abundance of F6P effects in a better attention of fructose 2,6-bisphosphate (F-2,6-BP).

Phosphofructokinase (PFK) is the enzyme that controls the 1/3 step of glycolysis, the conversion of fructose-6-phosphate (F6P) into fructose-1,6-biphosphate (F1,6BP). It works through shifting a phosphate institution from ATP to F6P. This is the slowest response in glycolysis and consequently is the rate-restricting step.

So, the answer is C. ATP and ADP.

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