N-acetylmuramic acid 6-phosphate etherase

N-acetylmuramic acid 6-phosphate etherase
Identifiers
EC number 4.2.1.126
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

N-acetylmuramic acid 6-phosphate etherase (EC 4.2.1.126, 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 proteobacteria.

References

  1. Jaeger, T.; Arsic, M.; Mayer, C. (2005). "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"". J. Biol. Chem. 280: 30100–30106. PMID 15983044. doi:10.1074/jbc.m502208200.
  2. Uehara, T.; Suefuji, K.; Valbuena, N.; Meehan, B.; Donegan, M.; Park, J.T. (2005). "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate". J. Bacteriol. 187: 3643–3649. PMC 1112033Freely accessible. PMID 15901686. doi:10.1128/jb.187.11.3643-3649.2005.
  3. Uehara, T.; Suefuji, K.; Jaeger, T.; Mayer, C.; Park, J.T. (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". J. Bacteriol. 188: 1660–1662. PMC 1367226Freely accessible. PMID 16452451. doi:10.1128/jb.188.4.1660-1662.2006.
  4. Hadi, T.; Dahl, U.; Mayer, C.; Tanner, M.E. (2008). "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling". Biochemistry. 47: 11547–11558. PMID 18837509. doi:10.1021/bi8014532.
  5. Jaeger, T.; Mayer, C. (2008). "N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism". Cell. Mol. Life Sci. 65: 928–939. PMID 18049859. doi:10.1007/s00018-007-7399-x.
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