Function
Enoylpyruvate transferase (MurA) or UDP-N-acetylglucosamine 1-carboxyvinyltransferase catalyzes the ligation of phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG). The pyruvate moiety makes the linker between the glycan and peptide portion of peptidoglycans. Thus MurA is essential for the biosynthesis of bacterial cell walls.[1].
- MurC or UDP-N-acetylmuramate-L-alanine ligase adds L-alanine in the biosynthesis of peptidoglycans which form part of the protective bacterial cell wall[2].
Relevance
MurA is a target for antibiotics such as fosfomycin.
Structural highlights
MurA is composed of catalytic domain and C-terminal domain. The active site is located at the interface of the two domains and binds the fosfomycin and UDP-GlcNAc.[3] Water molecules are shown as red spheres.
3D Structures of enoylpyruvate transferase
Enoylpyruvate transferase 3D structures
- ↑ Brown ED, Vivas EI, Walsh CT, Kolter R. MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J Bacteriol. 1995 Jul;177(14):4194-7. PMID:7608103
- ↑ Humnabadkar V, Prabhakar KR, Narayan A, Sharma S, Guptha S, Manjrekar P, Chinnapattu M, Ramachandran V, Hameed SP, Ravishankar S, Chatterji M. UDP-N-acetylmuramic acid l-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death. Antimicrob Agents Chemother. 2014 Oct;58(10):6165-71. doi: 10.1128/AAC.02890-14. , Epub 2014 Aug 11. PMID:25114134 doi:https://dx.doi.org/10.1128/AAC.02890-14
- ↑ Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure. 1996 Dec 15;4(12):1465-74. PMID:8994972
