Anhydro-N-acetylmuramic acid kinase
Anhydro-N-acetylmuramic acid kinase | |||||||||
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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 | ||||||||
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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
- ↑ 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. PMID 15901686.
- ↑ 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. PMID 16452451.
- ↑ 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. PMID 21288904.
External links
- Anhydro-N-acetylmuramic acid kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
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