Bacterial glycolytic and fermentative enzymes of dental plaque

Bacterial glycolytic and fermentative enzymes represent a group of metabolic proteins found in acidogenic oral bacteria, most notably Streptococcus mutans and Lactobacillus species. These enzymes, including enolase, lactate dehydrogenase (LDH), and pyruvate kinase, are responsible for the breakdown of dietary sugars into organic acids, primarily lactic acid (Takahashi & Nyvad, 2011). This metabolic process occurs within the dental plaque biofilm and is the primary driver of dental caries, as the resulting acid lowers the local pH and demineralizes tooth enamel (Marquis, 1995). Therapeutic strategies targeting these enzymes aim to disrupt the acidogenic potential of the biofilm. For example, fluoride ions directly inhibit enolase, a key glycolytic enzyme, by forming a complex with magnesium at the active site (Guha-Chowdhury et al., 1997). Additionally, sugar alcohols like xylitol act as competitive inhibitors of the phosphotransferase system (PTS), leading to a futile cycle that exhausts bacterial energy and reduces acid production (Nayak et al., 2014). Targeting these metabolic pathways is a cornerstone of preventive dentistry and oral health maintenance.

Other names

Oral bacterial metabolic enzymesDental plaque glycolytic enzymesAcidogenic bacterial enzymesGlycolytic enzymes of Streptococcus mutansFermentative enzymes of oral biofilm

Direct inhibition of key glycolytic enzymes such as enolase and lactate dehydrogenase, or competitive interference with sugar transport systems like the phosphotransferase system (PTS) to reduce acidogenic output.