Anhydro-N-acetylmuramic acid kinase

Anhydro-N-acetylmuramic acid kinase
Identifiers
EC number 2.7.1.170
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Anhydro-N-acetylmuramic acid kinase (EC 2.7.1.170, anhMurNAc kinase, AnmK) is an enzyme with systematic name ATP:1,6-anhydro-N-acetyl-beta-muramate 6-phosphotransferase.[1][2][3] This enzyme catalyses the following chemical reaction

ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O ADP + N-acetylmuramate 6-phosphate

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

References

  1. ↑ 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. doi:10.1128/jb.187.11.3643-3649.2005. PMC 1112033. PMID 15901686.
  2. ↑ 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. doi:10.1128/jb.188.4.1660-1662.2006. PMC 1367226. PMID 16452451.
  3. ↑ Bacik, J.P.; Whitworth, G.E.; Stubbs, K.A.; Yadav, A.K.; Martin, D.R.; Bailey-Elkin, B.A.; Vocadlo, D.J.; Mark, B.L. (2011). "Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase". J. Biol. Chem. 286: 12283–12291. doi:10.1074/jbc.m110.198317. PMC 3069431. PMID 21288904.
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