UDP-N-acetylglucosamine 1-carboxyvinyltransferase (IPR005750)

Short name: UDP_GlcNAc_COvinyl_MurA

Overlapping homologous superfamilies

Family relationships



The bacterial enzyme UDP-N-acetylglucosamine (UDP-GlcNAc) enolpyruvyltransferase (MurA) catalyzes the transfer of enolpyruvate from phosphoenolpyruvate to uridine diphospho-N-acetylglucosamine, which is the first committed step of bacterial cell wall biosynthesis. Experimental evidence suggests that binding of substrates to the enzyme does not exclusively follow an ordered mechanism with UDP-GlcNAc binding first, although binding of UDP-GlcNAc to free enzyme is preferred and possibly influenced by pyruvate-P. The reaction thus appears to follow an induced-fit mechanism, in which the binding site for fosfomycin, and presumably also for pyruvate-P, is created by the interaction of free enzyme with the sugar nucleotide [PMID: 13129913].

This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase (AroA) [PMID: 13129913].

GO terms

Biological Process

GO:0019277 UDP-N-acetylgalactosamine biosynthetic process

Molecular Function

GO:0008760 UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.