| Anhydro-N-acetylmuramic acid kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 use of anhydro- N-acetylmuramic acid in Pseudomonadota.
References
- ^ 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.
- ^ 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.
- ^ 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.
External links
- Anhydro-N-acetylmuramic+acid+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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