Enolase (ENO) (ENO)

Bacterial enolase, also known as phosphopyruvate hydratase, is a vital metalloenzyme in the glycolytic pathway of oral bacteria, most notably Streptococcus mutans (Source: UniProt P0A3E0). It catalyzes the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate, a key step in the fermentation process that produces lactic acid. In the oral cavity, the accumulation of this acid leads to the demineralization of tooth enamel and the development of dental caries (Source: PubMed PMID: 12672160). Beyond its metabolic function, enolase acts as a moonlighting protein on the bacterial cell surface, where it serves as a receptor for human plasminogen, facilitating bacterial adhesion and tissue colonization (Source: PubMed PMID: 23433376). The enzyme is a primary therapeutic target for fluoride, which inhibits its activity and effectively reduces the acidogenicity of dental plaque. Consequently, it is a central focus in preventive dentistry and the development of anti-caries agents.

Other names

Phosphopyruvate hydratase2-phospho-D-glycerate hydro-lyaseSurface-associated enolaseBacterial enolase

Fluoride ions inhibit bacterial enolase by forming a magnesium-fluorophosphate complex at the enzyme's active site, which displaces the required magnesium cofactor and prevents the conversion of 2-phosphoglycerate to phosphoenolpyruvate, thereby halting glycolysis and lactic acid production (Source: PubMed PMID: 12672160).