Bacterial glycolytic enzymes (Streptococcus mutans)

Bacterial glycolytic enzymes in Streptococcus mutans represent a critical suite of metabolic proteins that drive the pathogenicity of dental caries [NIH, 2024]. As a lactic acid bacterium, S. mutans relies almost exclusively on glycolysis for energy production, converting dietary sugars into lactic acid [Wikipedia, 2024]. This metabolic activity results in the acidification of the dental plaque environment, which promotes the demineralization of tooth enamel and the formation of carious lesions [NIH, 2022]. Key enzymes within this pathway, including enolase, lactate dehydrogenase (LDH), and pyruvate kinase, are established therapeutic targets [NIH, 2006]. For instance, fluoride inhibits enolase activity, while xylitol disrupts the phosphotransferase system (PTS), both leading to reduced acid production and impaired bacterial growth [Frontiers, 2022]. Targeting these enzymes allows for the modulation of bacterial virulence, although achieving selectivity to avoid harming beneficial commensal species remains a significant therapeutic challenge [NIH, 2023].

Other names

S. mutans glycolytic enzymesCariogenic bacterial glycolytic pathwayGlycolytic enzymes of Streptococcus mutans

Inhibition of specific enzymatic steps in the glycolytic pathway (e.g., enolase, lactate dehydrogenase, pyruvate kinase) or interference with sugar uptake (PTS), leading to reduced ATP production and decreased lactic acid secretion [NIH, 2006; Frontiers, 2022].