Enolazë

Enolazë is an enzyme that plays a crucial role in glycolysis, a fundamental metabolic pathway that breaks down glucose. Specifically, enolazë catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. This reaction involves the dehydration of 2-phosphoglycerate, removing a molecule of water and forming a high-energy phosphate bond in phosphoenolpyruvate. This high-energy compound is then readily utilized in the subsequent step of glycolysis to generate ATP, the primary energy currency of cells.

Enolazë is found in virtually all organisms, from bacteria to humans, highlighting its essential nature in cellular energy production. The enzyme typically requires a divalent metal ion, most commonly magnesium (Mg2+), as a cofactor for its catalytic activity. The three-dimensional structure of enolazë consists of two distinct domains.

In humans, the enolazë enzyme exists in several isoforms, encoded by different genes. The most common isoforms are enolazë-α, enolazë-β, and enolazë-γ. These isoforms can also form heterodimers, adding to the complexity of its expression and function. While its primary role is in glycolysis, enolazë has also been implicated in other cellular processes, including cell proliferation and survival. Its involvement in these diverse functions has led to research exploring its potential as a biomarker and therapeutic target in diseases such as cancer.