The Role of Enolase in Glycolysis and Beyond: Its Mechanism and Potential as a Biomarker

Enolase

Dehydration of 2-phosphoglycerate to phosphoenolpyruvate

Enolase is an enzyme that plays a key role in glycolysis, which is the process whereby glucose is broken down into pyruvate to produce energy. Specifically, enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PEP), which is the substrate for the final step in glycolysis.

The reaction catalyzed by enolase is:

2-phosphoglycerate ⇌ phosphoenolpyruvate + H2O

Enolase is a metalloenzyme, meaning it contains a metal ion cofactor required for its activity. In this case, enolase requires either magnesium or manganese as a cofactor.

Enolase is found in both prokaryotes and eukaryotes and is highly conserved across species. It is also involved in other biochemical pathways, such as gluconeogenesis and the metabolism of certain amino acids.

In addition to its role in metabolism, enolase has been implicated in other cellular processes, including cell adhesion, migration, and signaling. It has also been found in extracellular fluids and has been proposed as a potential biomarker for various diseases.

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