Research progress on the targeting of glutamate racemase of Streptococcus mutans

Abstract

Streptococcus mutans (S.mutans) is widely considered to be the major etiological factor responsible for dental caries in humans. Strategies selectively inhibiting the specific virulence factors associated with its cariogenicity are promising. Glutamate racemase (MurI) is a cofactor-independent enzyme that catalyzes the interconversion of L-glutamate to D-glutamate, one of the essential amino acids present in the peptidoglycan. As the indispensable enzyme in peptidoglycan biosynthesis, MurI has therefore been an attractive target for therapeutic interventions. In this review, the classifications, structures, inhibitors and genetic studies of MurI are systematically summarized. A comprehensive understanding of the relationship between MurI and cariogenic virulence of S.mutans can provide an important theoretical basis for potential therapeutic applications of dental caries. Key words: Glutamate racemase; Inhibitor; Gene deletion mutation; Cariogenic virulence