Enolase from cariogenic bacteria (Eno)

Cariogenic bacterial enolase is a highly conserved metalloenzyme (EC 4.2.1.11) found in caries-forming bacteria such as Streptococcus mutans. It catalyzes a critical step in glycolysis—the conversion of 2-phosphoglycerate to phosphoenolpyruvate—supporting bacterial metabolism under anaerobic, acidic conditions typical of dental biofilms. Enolase also exhibits 'moonlighting' functions, including involvement in RNA degradation complexes and serving as a plasminogen receptor on the bacterial surface, facilitating host interaction and colonization. Its essential role in bacterial survival, virulence, acid tolerance, and biofilm formation makes it a promising and validated target for the development of novel antimicrobial and anti-caries therapies. Potent small-molecule inhibitors, such as natural and synthetic tropolones, have demonstrated enolase inhibitory activity and bactericidal effects against cariogenic pathogens.

Other names

2-phospho-D-glycerate hydro-lyasePhosphopyruvate hydrataseEnoBacterial enolaseStreptococcal enolaseAlpha-enolase

Inhibition of enolase activity blocks glycolysis, compromising bacterial energy metabolism, especially under acidic, biofilm-forming conditions. Inhibitors may chelate the catalytic Mg²⁺ cofactors or bind to active site residues, preventing substrate (2-phosphoglycerate) conversion to product (phosphoenolpyruvate). For some agents (e.g., tropolones), interaction with the metalloenzyme active site inhibits catalytic function and thus impairs bacterial growth and survival.