Which molecule is known to cause allosteric feedback inhibition on hexokinase?

Hexokinase is an important enzyme in the glycolytic pathway, responsible for the phosphorylation of glucose to glucose 6-phosphate. Allosteric feedback inhibition is a regulatory mechanism where the end product of a pathway inhibits an upstream step to prevent the overproduction of that product.

In this case, glucose 6-phosphate acts as an allosteric inhibitor of hexokinase. When the concentration of glucose 6-phosphate rises, it indicates that there is already sufficient glucose being phosphorylated and, consequently, signals to the cell that less glucose should be converted into glucose 6-phosphate. This feedback mechanism helps regulate cellular metabolism by preventing excessive accumulation of glucose derivatives and maintaining metabolic balance.

Other molecules listed do not serve this specific allosteric feedback role for hexokinase. Fructose 1,6-bisphosphate, for example, is more involved in regulating phosphofructokinase, not hexokinase. Glucose 1-phosphate is a product of glycogenolysis and does not exert an allosteric effect on hexokinase. ATP, while it can signify energy status, acts predominantly as an allosteric inhibitor of phosphofructokinase, not hexokinase. Hence, glucose