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UDP-N-acetylglucosamine enolpyruvyl transferase

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UDP-N-acetylglucosamine enolpyruvyl transferase (or MurA) is an enzyme[1] that catalyzes the first committed step in peptidoglycan biosynthesis, namely the ligation of phosphoenolpyruvate (PEP) to the 3'-hydroxyl group of UDP-N-acetylglucosamine. This pyruvate moiety provides the linker that bridges the glycan and peptide portion of peptidoglycan.[2]

The enzyme is inhibited by the antibiotic fosfomycin, which covalently modifies an active site cysteine residue.[3]

References

  1. ^ "Enolpyruvate transferase, EPT family". Retrieved 2008-11-23.
  2. ^ Brown ED, Vivas EI, Walsh CT, Kolter R (July 1995). "MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli". J. Bacteriol. 177 (14): 4194–7. PMC 177162. PMID 7608103.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ King, Michael B. (2005). Lange Q & A. New York: McGraw-Hill, Medical Pub. Division. p. 298. ISBN 0-07-144578-1.