Enolase (2-phospho-D-glycerate hydro-lyase) (ENO) (ENO)

Enolase (EC 4.2.1.11) in cariogenic bacteria, such as Streptococcus mutans, is a vital glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (UniProt: P0C0H1). This enzymatic activity is essential for the production of lactic acid, which lowers the pH in the oral biofilm and leads to the demineralization of tooth enamel, the primary cause of dental caries (PubMed: 23586010). In addition to its metabolic role, bacterial enolase often functions as a moonlighting protein on the cell surface, where it acts as a receptor for human plasminogen and salivary proteins, thereby facilitating bacterial adhesion and colonization (PubMed: 16267356). Fluoride, the most common therapeutic agent for caries prevention, directly inhibits enolase by forming a complex with magnesium and phosphate in the enzyme active site, effectively halting acid production (PubMed: 3514359). While enolase is a promising target for antimicrobial therapy, its high degree of conservation across species necessitates the development of inhibitors that can selectively target bacterial enolase without affecting human isoforms to ensure safety.

Other names

Phosphopyruvate hydratase2-phosphoglycerate dehydrataseSurface enolaseEnoStreptococcus mutans enolase

Inhibition of the enzymatic conversion of 2-phosphoglycerate to phosphoenolpyruvate, thereby disrupting the glycolytic pathway and reducing the production of lactic acid by cariogenic bacteria (PubMed: 3514359).