The enzyme phosphofructokinase-1 (PFK-1) catalyses the transference of a phosphoryl group from ATP to fructose-6-phosphate (F6P), resulting in ADP and fructose-1,6-bisphosphate (FBP).

One of the most significant enzymes that regulates glycolysis is phosphofructokinase-1 (PFK-1). It is a four subunit allosteric enzyme regulated by several activators and inhibitors. Fructose 6-phosphate and ATP are converted to fructose 1,6-bisphosphate and ADP in the essential “committed” stage of glycolysis, catalysed by PFK-1.

Phosphofructokinase is allosterically activated by a high level of adenosine monophosphate (AMP), although the most effective activator is fructose 2,6-bisphosphate, generated from fructose-6-phosphate (F6P) by Phosphofructokinase 2 (PFK2). Therefore, a high quantity of fructose 2,6-bisphosphate is produced by an excess of F6P. The binding of fructose 2,6-bisphosphate improves the affinity of phosphofructokinase for F6P and reduces the inhibitory influence of ATP. The acceleration of glycolysis in the presence of sufficient glucose is an illustration of feedforward stimulation.

Read Also:

• Glycolysis
• Glycolysis: Important Points
• Glycolysis: An Introduction To Glycolytic Pathway

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