Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen and human salivary mucin MG2 when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity that may help the dissemination through oral tissues and entrance into the blood stream. (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. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. 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 bacterial cell surface. Belongs to the enolase family.