Anhydro-N-acetylmuramic acid kinase

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
Anhydro-N-acetylmuramic acid kinase
Identifiers
EC no.2.7.1.170
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

References

  1. 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.
  2. 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.
  3. Bacik JP, Whitworth GE, Stubbs KA, Yadav AK, Martin DR, Bailey-Elkin BA, Vocadlo DJ, Mark BL (April 2011). "Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase". The Journal of Biological Chemistry. 286 (14): 12283–91. doi:10.1074/jbc.m110.198317. PMC 3069431. PMID 21288904.


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