Which enzyme is activated by PFK-1?

Phosphofructokinase-1 (PFK-1) plays a crucial role in regulating glycolysis, specifically catalyzing the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This step is considered one of the key regulatory points of the glycolytic pathway and occurs in response to the energy needs of the cell.

The enzyme that is activated by PFK-1 is pyruvate kinase. Pyruvate kinase catalyzes the final step of glycolysis, converting phosphoenolpyruvate (PEP) into pyruvate while producing ATP. The activation of pyruvate kinase occurs as a part of the overall regulatory framework of glycolysis, where PFK-1 promotes the flow of metabolites through the pathway, signaling that the cell is favoring anaerobic metabolism or energy production through glycolysis.

As fructose-1,6-bisphosphate accumulates due to increased activity of PFK-1, it acts as an allosteric activator of pyruvate kinase, ensuring that there is a smooth transition and continuation of the glycolytic process toward the production of pyruvate and energy.

The other options, though involved in different pathways or