Bacterial enolase (ENO) (ENO)

Bacterial enolase (EC 4.2.1.11) is a critical glycolytic enzyme found in oral pathogens such as Streptococcus mutans, where it catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate (PubMed: 16530921). This enzyme is the primary target of fluoride, which acts as a non-competitive inhibitor by forming a magnesium-fluoride-phosphate complex that blocks the active site, thereby halting the production of lactic acid that causes tooth decay (PubMed: 11029668). Beyond its role in energy metabolism, bacterial enolase often functions as a moonlighting protein on the cell surface, binding human plasminogen to facilitate tissue invasion and immune evasion (PubMed: 19151191). This dual role makes it a significant factor in both localized dental caries and systemic infections like infective endocarditis (PubMed: 24103447). Consequently, it is a focal point for developing antimicrobial strategies aimed at disrupting oral biofilms and maintaining dental health (PubMed: 29454101).

Other names

2-phospho-D-glycerate hydro-lyasePhosphopyruvate hydrataseSurface-associated enolaseSenEno

Inhibition of the enzymatic conversion of 2-phosphoglycerate to phosphoenolpyruvate by forming a magnesium-fluoride-phosphate complex in the active site, which disrupts glycolysis and acid production (PubMed: 16530921).