Enolase (Streptococcus mutans) (Eno)

Streptococcus mutans enolase is a multifunctional moonlighting enzyme that plays a critical role in the metabolism and pathogenesis of the primary causative agent of dental caries. Within the cytoplasm, it catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic pathway, which is the main source of energy and acid production for the bacterium (UniProt: P0C064). On the cell surface, it acts as a primary adhesin by binding to human plasminogen, facilitating the colonization of oral tissues and potentially contributing to systemic infections like infective endocarditis (PubMed: 15107358). Because S. mutans relies on rapid acid production to demineralize tooth enamel, enolase is a major target for the anti-caries effects of fluoride, which directly inhibits the enzyme's activity (PubMed: 2189151). Beyond fluoride, it is being investigated as a potential vaccine target due to its high conservation and surface exposure (PubMed: 25605535). However, therapeutic development must account for the high structural homology between bacterial and human enolase to avoid potential off-target effects or autoimmune responses.

Other names

2-phospho-D-glycerate hydro-lyasePhosphopyruvate hydrataseSurface enolaseS. mutans enolaseMoonlighting enolase

Direct inhibition of the enolase enzyme by forming a metal-fluoride-phosphate complex at the active site, which halts the glycolytic pathway and reduces lactic acid production (PubMed: 2189151).