Oral bacterial enolase (ENO) (ENO)

Oral bacterial enolase is a central glycolytic enzyme that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate. In the oral cavity, it is a major contributor to the pathogenicity of bacteria such as Streptococcus mutans by facilitating the production of lactic acid, which causes tooth enamel demineralization (Lemos et al., 2019, PubMed). Beyond its metabolic role, the enzyme often functions as a moonlighting protein on the bacterial surface, where it acts as a receptor for human plasminogen and aids in bacterial adhesion to the dental pellicle (Nagano et al., 2012, PubMed). This dual role makes it a critical factor for both the survival and the virulence of cariogenic and periodontopathic biofilms. The enzyme is the primary target of fluoride, a widely used prophylactic agent that inhibits enolase by forming a magnesium-fluoride-phosphate complex in the active site (Marquis, 1995, PubMed). Inhibition of this enzyme effectively shuts down the glycolytic pathway, reducing the acidogenic potential of the oral biofilm. Other related metabolic enzymes, such as lactate dehydrogenase and F-ATPase, work in concert with enolase to maintain pH homeostasis and energy flux in oral pathogens. Research into novel small-molecule inhibitors of bacterial enolase continues to be a focus for developing next-generation anti-caries and anti-periodontitis treatments.

Other names

2-phospho-D-glycerate hydrolasePhosphopyruvate hydrataseBacterial enolaseStreptococcal enolaseOral bacterial glycolytic enzymes

Inhibition of enzyme activity through the formation of a magnesium-fluoride-phosphate complex in the active site, thereby blocking the glycolytic pathway and reducing acid production (Marquis, 1995, PubMed).