Bacterial glycosyltransferase

Bacterial glycosyltransferases are a large and diverse family of enzymes (commonly abbreviated as GTs; EC 2.4) that catalyze the transfer of sugar residues from activated donor molecules (such as UDP-glucose) to specific acceptor molecules, forming glycosidic bonds[1][5][7]. These enzymes are essential for the biosynthesis of disaccharides, oligosaccharides, polysaccharides, glycoproteins, glycolipids, and exopolysaccharides in bacteria[1][3][7]. Bacterial glycosyltransferases are involved in key biological processes such as cell wall synthesis (e.g., peptidoglycan, lipopolysaccharide, and capsule assembly), glycosylation of secreted and surface proteins, and in the production of virulence factors that mediate adhesion, immune evasion, and biofilm formation[3][4][5]. GTs are classified into more than 95 sequence-based families according to the Carbohydrate-Active enZYmes (CAZy) database[1][2][7]. They are regarded as potential antibacterial drug targets, but therapeutic exploitation is challenging due to structural diversity, processivity, and similarity with host enzymes[1][5][7]. Currently, there are no major clinically used GT inhibitors, but this enzyme class is seen as promising for future antimicrobial and antivirulence drug development[5].

Other names

GlycosyltransferaseGTGT enzymeBacterial GT

Inhibitors generally function by blocking the active site, mimicking donor or acceptor substrates, or interfering with enzyme-substrate binding[3][5]. Disruption of cell wall or capsule biosynthesis[3][4].