Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria. (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Catalytically active also when expressed on the bacterial cell surface. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. Homooctamer. Forms a ring-shaped structure. Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface, probably in complex with plasminogen. Belongs to the enolase family.