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. MurA is composed of catalytic domain and C-terminal domain[1].
Relevance
MurA is a target for antibiotics such as fosfomycin.
3D Structures of enoylpyruvate transferase
Updated on 19-January-2016
References
↑ 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
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