Phosphopyruvate hydratase

Phosphopyruvate hydratase, also known as Enolase, is an enzyme that catalyzes the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. This enzyme is a homodimer and is found in a wide range of organisms, from bacteria to humans.

Structure

Phosphopyruvate hydratase is a protein made up of two identical subunits. Each subunit is composed of a single polypeptide chain, which folds into a compact, globular structure. The active site of the enzyme, where the catalytic reaction takes place, is located at the interface between the two subunits.

Function

The primary function of phosphopyruvate hydratase is to catalyze the dehydration of 2-phosphoglycerate to phosphoenolpyruvate in the glycolytic pathway. This reaction is reversible, and the enzyme can also catalyze the reverse reaction, the hydration of phosphoenolpyruvate to 2-phosphoglycerate, in the gluconeogenesis pathway.

Clinical significance

Mutations in the gene encoding phosphopyruvate hydratase can lead to Enolase deficiency, a rare metabolic disorder. Symptoms of this disorder can include developmental delay, seizures, and muscle weakness. In addition, phosphopyruvate hydratase has been implicated in several types of cancer, as its activity is often increased in cancer cells.

See also

• Glycolysis
• Enzyme
• Enolase deficiency
• Gluconeogenesis