Streptococcus mutans ADP-glucose pyrophosphorylase (ADP-Glc PPase)

Streptococcus mutans ADP-glucose pyrophosphorylase (ADP-Glc PPase) is a key regulatory enzyme in the biosynthesis of intracellular polysaccharides (IPS), which are glycogen-like polymers [1, 15]. This enzyme, encoded by the glgC and glgD genes, catalyzes the conversion of ATP and glucose-1-phosphate into ADP-glucose and inorganic pyrophosphate [1, 19]. In S. mutans, IPS serves as a critical energy reserve that the bacterium utilizes during periods of sugar starvation to produce lactic acid [1, 27]. This prolonged acid production leads to the demineralization of tooth enamel, making ADP-Glc PPase a significant virulence factor in the development of dental caries [8, 20]. Because this enzyme is absent in humans and plays a vital role in the cariogenic potential of the pathogen, it is considered a promising therapeutic target [21]. Compounds such as monofluorophosphate (MFP), a common additive in dental care products, have been shown to inhibit this enzyme, thereby reducing IPS accumulation and the subsequent risk of tooth decay [20, 22].

Other names

Glucose-1-phosphate adenylyltransferaseATP:alpha-D-glucose-1-phosphate adenylyltransferaseGlgCGlgD

Inhibition of ADP-glucose synthesis, leading to reduced intracellular polysaccharide (IPS) accumulation and decreased acid production.