Streptococcus mutans glycolytic enzymes

Streptococcus mutans glycolytic enzymes represent a suite of metabolic proteins essential for the survival and pathogenicity of the primary dental caries-causing bacterium, Streptococcus mutans [PMID: 30713038]. These enzymes, including enolase, lactate dehydrogenase (LDH), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), facilitate the Embden-Meyerhof-Parnas pathway, converting dietary sugars into lactic acid. This acid production (acidogenesis) is the direct cause of tooth enamel demineralization and subsequent cavity formation [PMID: 16461665]. Because S. mutans relies almost exclusively on glycolysis for ATP production, these enzymes are attractive therapeutic targets. Drugs like fluoride effectively inhibit enolase, while various polyphenols and small molecules target LDH to reduce acid output [PMID: 12144470, PMID: 23821264]. Targeting this pathway aims to disrupt the energy metabolism and virulence of cariogenic biofilms without necessarily relying on broad-spectrum bactericidal action.

Other names

Streptococcus mutans glycolytic pathwayEmbden-Meyerhof-Parnas pathway enzymes in Streptococcus mutansAcidogenic enzymes of Streptococcus mutans

The primary mechanism involves the competitive or non-competitive inhibition of key enzymes such as enolase, lactate dehydrogenase, and pyruvate kinase. For example, fluoride ions form a complex with magnesium at the active site of enolase, preventing the conversion of 2-phosphoglycerate to phosphoenolpyruvate [PMID: 12144470]. Other inhibitors like epigallocatechin gallate (EGCG) interfere with the activity of lactate dehydrogenase, thereby reducing the conversion of pyruvate to lactic acid [PMID: 23821264].