UDP-N-acetylglucosamine:N-acetylmuramyl-(pentapeptide) transferase (MurG)

MurG is an essential glycosyltransferase enzyme found in almost all bacteria, catalyzing the last cytoplasmic step in peptidoglycan biosynthesis. It transfers an N-acetylglucosamine (GlcNAc) moiety from UDP-GlcNAc to Lipid I, forming Lipid II, a crucial precursor for cell wall assembly[1][7][8]. Structurally, MurG consists of two α/β domains and operates as a peripheral membrane protein, associating with cell membrane phospholipids through a hydrophobic patch surrounded by basic residues[2][8]. MurG participates in multiprotein complexes with other cell wall synthesis enzymes (such as MraY, RodA, and penicillin-binding proteins), and its activity is tightly regulated during bacterial growth and division[3][5][6]. Due to its universal and essential role in bacterial physiology, MurG is an attractive target for new antibiotics, with multiple studies exploring potential inhibitor interactions—most notably, flavonoids like quercetin have demonstrated binding and inhibition in simulation and experimental models[4][6]. Blockade of MurG prohibits Lipid II formation, rendering bacteria unable to maintain a functional cell wall, leading to lysis and cell death.

Other names

MurG glycosyltransferasePeptidoglycan glycosyltransferase MurGUDP-GlcNAc transferase MurG

Inhibition blocks formation of peptidoglycan precursors, leading to impaired cell wall synthesis and bacterial death