Hormonal regulation: insulin stimulates synthesis of more hexokinase
Phosphofructokinase 1:
Phosphorylates fructose 6-phosphate into fructose 1,6-bisphosphate
Highly regulated step in glycolysis
Inhibited by ATP and citrate
Stimulated by high levels of ADP
Pyruvate kinase:
Converts phosphoenolpyruvate (PEP) into pyruvate
Stimulated by fructose 1,6-bisphosphate
Inhibited by ATP and alanine
High amounts of ADP stimulate the enzyme to signal low ATP levels and stimulate ATP production
Fructose 6-phosphate can be converted into fructose 2,6-bisphosphate by a heteronuclear enzyme complex consisting of phosphofructokinase 2 and fructose 2,6-bisphosphatase
Fructose 2,6-bisphosphate is a powerful regulator of phosphofructokinase 1, stimulating the enzyme to convert more fructose 6-phosphate into fructose 1,6-bisphosphate to make ATP
Insulin stimulates the enzyme pyruvate kinase by removing phosphates, while glucagon inhibits it by phosphorylating the enzyme
Inhibition of pyruvate kinase can occur with high ATP levels, long-chain fatty acyl CoAs, and too much acetyl CoA, indicating excessive energy production
Fructose 1,6-bisphosphate acts as a feed-forward stimulator, preparing pyruvate kinase for increased activity in glycolysis
Glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase are susceptible to inhibition by arsenate, which can bind in the place of phosphate and disrupt the enzyme's function