Biology: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". http://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=55209. Retrieved 2008-11-23. 
  2. ↑ "MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli". J. Bacteriol. 177 (14): 4194–7. July 1995. PMID 7608103. 
  3. ↑ King, Michael B. (2005). Lange Q & A. New York: McGraw-Hill, Medical Pub. Division. pp. 298. ISBN 0-07-144578-1. https://archive.org/details/langeqausmlestep0005unse/page/298. 




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