Bacterial glycolytic enzymes and F-ATPases

Bacterial glycolytic enzymes and F-ATPases in oral bacteria are critical metabolic components of cariogenic pathogens like Streptococcus mutans [1]. Glycolytic enzymes, such as enolase and phosphoglycerate mutase, are responsible for converting dietary sugars into lactic acid, which lowers the pH of the oral environment and leads to tooth enamel demineralization [2]. F-ATPases (F1F0-ATPases) function as proton-translocating pumps that expel hydrogen ions from the bacterial cell, allowing these organisms to maintain internal pH homeostasis and survive in the acidic conditions they produce [3]. Fluoride is the most prominent therapeutic agent targeting these systems; it directly inhibits enolase and interferes with F-ATPase activity, often by forming inhibitory complexes with metal ions like magnesium or aluminum [1,2]. This dual inhibition effectively reduces both the acidogenicity (acid production) and aciduricity (acid tolerance) of the oral biofilm [3]. Consequently, these enzymes and transporters are primary targets for preventive dental treatments aimed at controlling dental caries and maintaining oral health.

Other names

Oral bacterial metabolic enzymesGlycolytic pathway enzymesProton-translocating F-type ATPaseCariogenic bacterial enzymes

Inhibition of enolase activity and disruption of F-ATPase-mediated proton export, leading to reduced acid production and impaired acid tolerance in oral pathogens.