Enoylpyruvate transferase

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spinqualitylabelsall models Structure of enoylpyruvate transferase complex with fosfomycin and UDP-N-acetylglucosamine (PDB entry 3kr6) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Enoylpyruvate transferase (MurA) 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]. Relevance MurA is a target for antibiotics such as fosfomycin. Structural highlights MurA is composed of and . The active site is located at the interface of the two domains and binds the and .[2] Water molecules are shown as red spheres.

3D Structures of enoylpyruvate transferase

Updated on 11-March-2019

References

1. ↑ 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
2. ↑ 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