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The activity of phosphofructokinase 1 is increased by the binding ofGroup of answer choicesATPADPCitrateAcetyl CoATwo or more of the above

Question

The activity of phosphofructokinase 1 is increased by the binding ofGroup of answer choicesATPADPCitrateAcetyl CoATwo or more of the above

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Solution

Phosphofructokinase 1 (PFK1) is a key enzyme in the glycolytic pathway. It is regulated by several metabolites, with ATP and citrate being known inhibitors and ADP being a known activator.

Here are the steps to answer your question:

  1. ATP: ATP is an inhibitor of PFK1. When ATP levels are high, it binds to PFK1 and decreases its activity. This makes sense because high ATP levels signal that the cell has enough energy, so it doesn't need to break down more glucose through glycolysis.

  2. ADP: ADP is an activator of PFK1. When ADP levels are high, it binds to PFK1 and increases its activity. This is because high ADP levels signal that the cell needs more energy, so it needs to break down more glucose through glycolysis.

  3. Citrate: Citrate is an inhibitor of PFK1. When citrate levels are high, it binds to PFK1 and decreases its activity. This is because high citrate levels signal that the cell has enough building blocks for the citric acid cycle, so it doesn't need to break down more glucose through glycolysis.

  4. Acetyl CoA: Acetyl CoA does not directly regulate PFK1. However, it is a product of glycolysis and can be used in the citric acid cycle to produce ATP.

So, the answer to your question is "ADP".

This problem has been solved

Similar Questions

What statements are TRUE?  Phosphofructokinase (PFK) is:i) activated by elevated ATP/ADP ratiosii) activated by AMPiii) inhibited by AMPiv) requires fructose 6 phosphatev) a rate limiting enzyme of glycolysisvi) reversiblevii) the commitment step in glycolysisviii) requires ATP

Question 2. Phosphofructokinase1 The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a give concentration of Fructose-6- phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? b) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the diagram. How can this observation be explained?

Phosphofructokinase-1 converts Fructose 6-phosphate to Fructose 1,6- bisphosphate. Which statement about the reaction is CORRECT? Under anaerobic conditions, this reaction plays an important role in regenerating NAD+ for use in the “pay-off” phase of glycolysis. This reaction occurs in the cytoplasm and is performed by an enzyme shared between glycolysis and gluconeogenesis. This is a readily reversible reaction which is allosterically regulated by Fructose 1,6- bisphosphate. The bifunctional PFK-2/FBPase-2 enzyme controls the concentration of the allosteric regulator of this reaction.

n glycolysis, hexokinase is inhibited by a buildup of which product?*

(iv) State the basicity of phosphoric acid.

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