fosfofruktokináza1

Phosphofructokinase-1, often abbreviated as PFK-1, is a crucial enzyme in cellular metabolism. It plays a central role in glycolysis, the metabolic pathway that breaks down glucose to produce energy in the form of ATP. Specifically, PFK-1 catalyzes the irreversible conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This step is considered a major regulatory point in glycolysis.

The activity of PFK-1 is tightly controlled by various allosteric effectors. ATP is a key regulator, acting as both a substrate and an inhibitor. When ATP levels are high, it binds to PFK-1 and reduces its activity, signaling that the cell has sufficient energy. Conversely, AMP, a product of ATP hydrolysis, acts as an activator, indicating low energy levels and promoting glycolysis. Citrate, an intermediate in the citric acid cycle, also inhibits PFK-1, suggesting that the cell has enough intermediates for energy production. Fructose-2,6-bisphosphate is a potent activator of PFK-1, significantly increasing its affinity for fructose-6-phosphate and driving glycolysis forward, especially when glucose is abundant.

Deficiencies in PFK-1 can lead to a rare genetic disorder known as Glycogen Storage Disease type VII, also called Tarui's disease. This condition affects muscles and red blood cells, leading to symptoms such as muscle cramps, weakness, and hemolytic anemia due to impaired glycolysis. The enzyme's critical role in energy production makes its proper functioning essential for cellular health.