Hexokinase is inhibited by its product, glucose-6-phosphate.

Phosphofructokinase is activated by elevated levels of AMP and inhibited by elevated concentrations of ATP, citrate, and low pH, but the predominant allosteric regulator of this enzyme is fructose-2,6-bisphosphate. Phosphofructokinase-2 synthesizes fructose-2,6-bisphosphate and is activated by PKA and inhibited by PP1. TIGAR breaks down fructose-2,6-bisphosphate inhibiting phosphofructokinse.

Pyruvate kinase is activated by the allosteric regulator fructose-1,6-bisphosphate. It is inhibited by elevated concentrations of acetyl-CoA, ATP, and the amino acid alanine. Pyruvate kinase in liver is also inhibited by phosphorylation (via PKA) and activated by dephosphorylation (via PP1).

Pyruvate carboxylase is activated by elevated concentrations of acetyl-CoA in mitochondria.

Fructose-1,6-bisphosphatase is inhibited by the allosteric regulators AMP and fructose-2,6-bisphosphate.

Pyruvate dehydrogenase is inhibited by elevated levels of acetyl-CoA and NADH. It is also inhibited by phosphorylation (via Pyruvate Dehydrogenase Kinase) and activated by dephosphorylation (via Pyruvate Dehydrogenase Phosphatase).