(R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming)

N-acetylmuramic acid 6-phosphate etherase
EC no.
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

N-acetylmuramic acid 6-phosphate etherase (EC, MurNAc-6-P etherase, MurQ) is an enzyme with systematic name (R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate N-acetylmuramate 6-phosphate + H2O

This enzyme is required for the utilization of anhydro-N-acetylmuramic acid in some proteobacteria.


  1. ^ Jaeger T, Arsic M, Mayer C (August 2005). "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"". The Journal of Biological Chemistry. 280 (34): 30100–6. doi:10.1074/jbc.m502208200. PMID 15983044.
  2. ^ Uehara T, Suefuji K, Valbuena N, Meehan B, Donegan M, Park JT (June 2005). "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate". Journal of Bacteriology. 187 (11): 3643–9. doi:10.1128/jb.187.11.3643-3649.2005. PMC 1112033. PMID 15901686.
  3. ^ Uehara T, Suefuji K, Jaeger T, Mayer C, Park JT (February 2006). "MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall". Journal of Bacteriology. 188 (4): 1660–2. doi:10.1128/jb.188.4.1660-1662.2006. PMC 1367226. PMID 16452451.
  4. ^ Hadi T, Dahl U, Mayer C, Tanner ME (November 2008). "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling". Biochemistry. 47 (44): 11547–58. doi:10.1021/bi8014532. PMID 18837509.
  5. ^ Jaeger T, Mayer C (March 2008). "N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism". Cellular and Molecular Life Sciences. 65 (6): 928–39. doi:10.1007/s00018-007-7399-x. PMID 18049859.

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