EC 4.2.1.126 - N-acetylmuramic acid 6-phosphate etherase

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IntEnz Enzyme Nomenclature
EC 4.2.1.126

Names

Accepted name:
N-acetylmuramic acid 6-phosphate etherase
Other names:
MurNAc-6-P etherase
MurQ
Systematic name:
(R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming)

Reaction

Comments:

This enzyme, along with EC 2.7.1.170, anhydro-N-acetylmuramic acid kinase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (204) [show] [UniProt]

References

  1. Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M., Park, J. T.
    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 (2005). [PMID: 15901686]
  2. Uehara, T., Suefuji, K., Jaeger, T., Mayer, C., Park, J. T.
    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 (2006). [PMID: 16452451]
  3. Jaeger, T., Arsic, M., Mayer, C.
    Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase".
    J. Biol. Chem. 280: 30100-30106 (2005). [PMID: 15983044]
  4. Hadi, T., Dahl, U., Mayer, C., Tanner, M. E.
    Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling.
    Biochemistry 47: 11547-11558 (2008). [PMID: 18837509]
  5. Jaeger, T., Mayer, C.
    N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism.
    Cell. Mol. Life Sci. 65: 928-939 (2008). [PMID: 18049859]

[EC 4.2.1.126 created 2011]