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Phosphofructokinase catalyzes the first reaction in a pathway that commits the product to proceed through glycolysis, often called the first commitment step in glycolysis. Phosphofructokinase is also regulated so that the cell can quickly respond to its energy needs. Given this background information about phosphofructokinase, what is the most likely mode of inactivation of this enzyme when the cell needs to slow down or turn off glycolysis?

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Answer:

Dephosphorylation of the enzyme

Step-by-step explanation:

Being an enzyme that is activated by coupling it with a phosphor, that is to say, by phosphorylating it, by means of a kinase, this will be inactive if it is defformed with an enzyme that is responsible for breaking the union between the enzyme and the phosphorus.

This is how most of the enzymes that make up our enzymatic digestive system can be controlled, it is important to take into account that those that are phosphorylatable, as soon as the phosphorus is uncoupled from them, they will enter an inactive state and will not catalyze the metabolite, or it will not run the chemical reaction.

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