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].
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
Enoylpyruvate transferase 3D structures
