UDP-N-acetylmuramoyl-L-alanine–D-glutamate ligase (MurD)

UDP-N-acetylmuramoyl-L-alanine–D-glutamate ligase (MurD) is an essential cytoplasmic enzyme in bacteria that catalyzes the ATP-dependent addition of D-glutamic acid to UDP-N-acetylmuramoyl-L-alanine, producing UDP-N-acetylmuramoyl-L-alanine–D-glutamate, a critical step in peptidoglycan precursor biosynthesis. MurD, along with MurC, MurE, and MurF, forms a family of peptidoglycan peptide ligases responsible for sequentially adding amino acids to the glycan backbone precursor. These enzymatic steps are vital for maintaining bacterial cell wall integrity and survival. MurD's essential role in bacterial viability and absence in mammals make it an attractive and validated target for new antibacterial agents, although no clinically approved inhibitors exist yet[2][3][7]. The enzyme has been extensively studied in structural and mechanistic terms, facilitating rational drug design efforts.

Other names

MurDD-glutamic acid–adding enzymeUDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Inhibition of MurD prevents the addition of D-glutamic acid to UDP-MurNAc-L-Ala, blocking peptidoglycan synthesis and leading to bacterial cell death[2][3].