High levels of ATP inhibit PFK
No, it is not true. PEP, or phosphoenolpyruvate, is actually a substrate for phosphofructokinase (PFK), a key enzyme in glycolysis. PEP is converted to fructose-1,6-bisphosphate by PFK, which is an important step in the glycolytic pathway.
Phosphofructokinase-1 (PFK-1)
Loss of allosteric binding site for ATP on phosphofructokinase-1 (PFK-1)
Phosphofructokinase (PFK)
ATP inhibiting PFK-1 (phosphofructokinase-1)
PFK can refer to phosphofructokinase, an enzyme involved in glycolysis, a metabolic pathway that converts glucose into energy. It can also stand for People for Kids, an organization that focuses on advocating for children's rights and well-being.
Some abbreviations for enzymes involved in the breakdown of glucose are HK (hexokinase), GK (glucokinase), PFK (phosphofructokinase), PK (pyruvate kinase), and G6Pase (glucose-6-phosphatase).
Citrate acts as an inhibitor of phosphofructokinase (PFK), which is a key enzyme in glycolysis. When citrate levels are high, it indicates that the cell has sufficient energy and metabolic intermediates, leading to the inhibition of PFK to prevent excessive glucose breakdown. This regulatory mechanism helps maintain energy balance within the cell.
Phosphofructokinase is an enzyme that plays a key role in glycolysis, the metabolic pathway that breaks down glucose to produce energy. It helps regulate the rate of glycolysis by catalyzing the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This enzyme is critical for energy production in cells.
Fructose-6-phosphate to fructose 1,6-bisphosphate. Phosphofructokinase (PFK). Requires ATP, Mg. First majorly regulated step of glycolysis. Irreversible
Phosphofructokinase
PFK Piešťany was created in 1912.