EC Number   |
General Information |
Reference |
|---|
   2.7.1.170 | evolution |
1,6-anhydro-N-acetylmuramic acid kinase (AnmK) and levoglucosan kinase (LGK) share significant sequence homology (30-40%) and form a subfamily of anhydrosugar kinases in the sugar kinase family, which is itself part of a larger superfamily of ATPase domain containing proteins (sugar kinase/heat shock protein 70/actin superfamily) that contain conserved structural motifs including the ATP binding domain and an interdomain hinge region that allows the two major domains to rotate relative to each other |
738435 |
| 2.7.1.170 | evolution |
althoughAnmKadopts a two-domain fold that is structurally similar to proteins of the hexokinase-hsp70-actin superfamily, 1,6-anhydrosugar kinases are mechanistically unique in that they catalyze both the hydrolysis of the 1,6-anhydro ring and the transfer of the gamma-phosphate group from ATP to O6 of sugar substrates |
738636 |
| 2.7.1.170 | evolution |
phylogenetic analysis and comparison of 1,6-anhydro-N-acetylmuramic acid kinase with levoglucan kinase and AnmK-like enzymes, molecular docking, dynamics simulation, and homology modelling, overview. AnmK and LGK are conserved proteins, and 187Asp, 212Asp are enzymatic residues, respectively |
-, 738937 |
| 2.7.1.170 | metabolism |
1,6-anhydro-N-acetylmuramic acid is produced during peptidoglucan degeneration by transglycosylases, e.g. AmpD or NagZ. The AnmK reaction product N-acetylmuramate 6-phosphate returns into peptidoglycan recycling |
738435 |
| 2.7.1.170 | more |
analysis of structures of enzyme AnmK bound to the reaction product ADP and the substrate anhMurNAc as well as the positioning of a conserved aspartate residue (Asp182) in the active site, prediction of a mechanism of catalysis for this enzyme. Conformational dynamics of AnmK during its catalytic cycle from subsequent structural studies of AnmK in the open conformation as well as small-angle X-ray scattering analysis of the enzyme. In solution the enzyme may adopt an open conformation when bound to either AMPPCP or without nucleotide present, while it adopts a more compact globular conformation in the presence of ADP, suggestive of a closed state. Dramatic conformational dynamics for AnmK, whereby it cycles between a closed catalytically competent state and an open state that likely facilitates substrate binding and product departure |
738435 |
| 2.7.1.170 | more |
the peptidoglycan recycling enzyme 1,6-anhydro-N-acetylmuramic acid kinase from Pseudomonas aeruginosa undergoes large conformational changes during its catalytic cycle, with its two domains rotating apart by up to 32° around two hinge regions to expose an active site cleft into which the substrates 1,6-anhydroMurNAc and ATP can bind. Ligand binding at the active site of AnmK coordinates its conformational itinerary |
738636 |
| 2.7.1.170 | more |
three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview |
738937 |
| 2.7.1.170 | physiological function |
enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic |
738435 |
| 2.7.1.170 | physiological function |
MurQ and AnmK kinase are required for utilization of 1,6-anhydro-N-acetyl-beta-muramate derived either from cell wall murein or imported from the medium |
715356 |
