2.7.1.170: anhydro-N-acetylmuramic acid kinase
This is an abbreviated version!
For detailed information about anhydro-N-acetylmuramic acid kinase, go to the full flat file.
Word Map on EC 2.7.1.170
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2.7.1.170
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levoglucosan
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adp
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bioconversion
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anhydrosugars
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biofuel
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murein
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peptidoglycan
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aeruginosa
- 2.7.1.170
- levoglucosan
- adp
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bioconversion
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anhydrosugars
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biofuel
- murein
- peptidoglycan
- aeruginosa
Reaction
Synonyms
1,6-anhydro-N-acetylmuramic acid kinase, anhMurNAc kinase, anhydro-N-acetylmuramic acid kinase, AnmK, YdhH
ECTree
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General Information on EC 2.7.1.170 - anhydro-N-acetylmuramic acid kinase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
physiological function
additional information
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
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
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
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
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
evolution
Shewanella oneidensis MR-1 / ATCC 700550
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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
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physiological function
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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
physiological function
enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic
physiological function
enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic
additional information
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
additional information
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
additional information
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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
additional information
three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview
additional information
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three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview
