Phospho-N-acetylmuramoyl-pentapeptide-transferase (MraY)

Phospho-N-acetylmuramoyl-pentapeptide-transferase (MraY) is an essential integral membrane enzyme in bacteria that catalyzes the first membrane-associated step in peptidoglycan biosynthesis, transferring the peptidoglycan precursor from UDP-N-acetylmuramoyl-pentapeptide (UDP-MurNAc-pentapeptide) to undecaprenyl phosphate to form lipid I[1][4][5][8]. This reaction initiates a sequence of lipid-linked steps required for assembling the bacterial cell wall, a process vital for bacterial growth and viability[2][3][7]. MraY is the molecular target of several classes of natural antibiotics and has become a major focus in new antibacterial drug development due to its absence in eukaryotes and its essential role in bacterial physiology[7][2]. Inhibitors of MraY block the formation of lipid I, effectively arresting bacterial cell wall construction and resulting in bactericidal activity. Notable inhibitors include tunicamycin and several natural product antibiotic classes, though clinical development is challenged by potential cytotoxicity in non-bacterial cells.

Other names

Phospho-N-acetyl-muramyl-pentapeptide translocaseTranslocase 1UDP-MurNAc-pentapeptide:undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferaseEC 2.7.8.13

Inhibition of peptidoglycan precursor transfer from UDP-MurNAc-pentapeptide to undecaprenyl phosphate, blocking initial step in bacterial cell wall synthesis[7][3][2].