Enolase (Phosphopyruvate hydratase) (ENO)

Bacterial enolase, or phosphopyruvate hydratase, is a highly conserved enzyme essential for the glycolytic pathway, where it catalyzes the reversible dehydration of 2-phosphoglycerate to phosphoenolpyruvate (PubMed: 11133477). In oral biofilm bacteria such as Streptococcus mutans, this metabolic activity is a primary source of the lactic acid that causes dental enamel demineralization and subsequent caries (PubMed: 15184351). Beyond its cytoplasmic role in energy production, enolase is frequently found on the bacterial cell surface, where it functions as a "moonlighting" protein that binds host plasminogen and extracellular matrix components (PubMed: 24508251). This surface localization facilitates bacterial adhesion, colonization, and the structural integrity of the oral biofilm, while also aiding in tissue invasion and immune evasion (UniProt: P0C0H4). Fluoride, the most common therapeutic agent targeting oral bacteria, acts by inhibiting enolase through the formation of a magnesium-fluoride-phosphate complex in the active site, effectively halting acid production and bacterial growth (StatPearls: Fluoride). Consequently, bacterial enolase represents a dual-purpose target for both metabolic inhibition and the disruption of pathogenic biofilm formation in dental and periodontal health.

Other names

2-phospho-D-glycerate hydro-lyasePhosphopyruvate hydrataseSurface-associated enolase2-phosphoglycerate dehydrataseEno

Inhibition of the enzymatic conversion of 2-phosphoglycerate to phosphoenolpyruvate, which disrupts the glycolytic pathway and reduces the production of cariogenic lactic acid (PubMed: 11133477).