Streptococcus mutans glycolytic and proton-pumping enzymes

Streptococcus mutans glycolytic and proton-pumping enzymes represent a critical suite of metabolic proteins that drive the pathogenesis of dental caries. The glycolytic enzymes, most notably enolase (phosphopyruvate hydratase) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are responsible for the rapid fermentation of dietary carbohydrates into lactic acid, which lowers the local pH and demineralizes tooth enamel [1][2]. To survive this self-induced acidic environment, S. mutans employs F-type H+-ATPases (proton pumps) that actively transport protons out of the cell to maintain internal pH homeostasis [3]. These enzymes are the primary pharmacological targets of fluoride, which acts as a direct inhibitor of enolase by forming a magnesium-fluorophosphate complex and indirectly impairs the H+-ATPase by increasing membrane permeability to protons [4]. Other antimicrobial agents like chlorhexidine and stannous ions also interact with these metabolic pathways to reduce bacterial acid production [5]. Targeting these enzymes effectively reduces the virulence of S. mutans by compromising its ability to produce acid and tolerate low-pH environments [1][3]. Citations: [1] Hamilton, I. R. (1990). J Dent Res. [2] Guha-Chowdhury, N., et al. (1997). J Dent Res. [3] Matsui, R., & Cvitkovitch, D. (2010). Future Microbiol. [4] Marquis, R. E. (1995). FEMS Microbiol Rev. [5] Takahashi, N., & Nyvad, B. (2011). J Dent Res.

Other names

S. mutans metabolic enzymesAcid-tolerance enzymesEnolase and F-ATPase complexGlycolytic pathway enzymesAcidogenic and aciduric enzymes

Inhibition of enolase activity through the formation of a metal-fluoride-phosphate complex and disruption of the F-type H+-ATPase proton pump to impair acid tolerance and metabolic activity.