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Literature summary for 2.7.1.170 extracted from
- Bioconversion of anhydrosugars: emerging concepts and strategies (2016), IUBMB Life, 68, 700-708.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene anmK, recombinant expression in Escherichia coli | Pseudomonas aeruginosa |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| analysis of several crystal structures | Pseudomonas aeruginosa |
| crystal structure analysis | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D182A | site-directed mutagenesis, inactive catalytic site mutant | Pseudomonas aeruginosa |
| D182N | site-directed mutagenesis, inactive catalytic site mutant | Pseudomonas aeruginosa |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Escherichia coli |  |
| ADP | - |
Pseudomonas aeruginosa | |
| additional information | no inhibition by N-acetylmuramate up to 20 mM | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | - |
1,6-anhydro-N-acetyl-beta-muramate | pH and temperature not specified in the publication | Pseudomonas aeruginosa | |
| 1 | - |
ATP | pH and temperature not specified in the publication | Escherichia coli | |
| 1 | - |
1,6-anhydro-N-acetyl-beta-muramate | pH and temperature not specified in the publication | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Pseudomonas aeruginosa | |
| Mg2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | Pseudomonas aeruginosa | 1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | Escherichia coli | 1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P77570 | gene anmK | - |
| Pseudomonas aeruginosa | Q9I5Q5 | gene anmK | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate | the oxygen of 1,6-anhydro-N-acetyl-beta-muramate, that is to be phosphorylated, is trapped in the anhydro ring structure and must first be cleaved prior to phosphorylation. In order to do this, Asp182 is predicted to act as a base to deprotonate a water molecule and enhance its nucleophilicity. The water would then attack the anomeric carbon of the sugar concomitant with transfer of the gamma-phosphate of ATP. The lone pair electrons from the O5 position would assume partial double-bond characteristics and stabilize the oxocarbenium ion that would otherwise develop, with the anomeric carbon adopting an axial conformation in the product acetylmuramate 6-phosphate, catalytic role of the conserved residue Asp182 residue in catalysis | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | - |
Pseudomonas aeruginosa | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | - |
Escherichia coli | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | 1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide | Pseudomonas aeruginosa | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
| ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O | 1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide | Escherichia coli | ADP + N-acetyl-beta-muramate 6-phosphate + H+ | - |
? | |
| additional information | the enzyme utilizes an unusual mechanism whereby the sugar substrate is both cleaved and phosphorylated. N-acetylmuramate cannot be used as a substrate for AnmK | Pseudomonas aeruginosa | ? | - |
? | |
| additional information | the enzyme utilizes an unusual mechanism whereby the sugar substrate is both cleaved and phosphorylated. N-acetylmuramate cannot be used as a substrate for AnmK | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | the enzyme structure exhibits two major domains separated by a deep hinge region with the nucleotide and sugar binding near the hinge. The protein forms a dimer, with extensive interactions between the two monomers | Pseudomonas aeruginosa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 1,6-anhydro-N-acetylmuramic acid kinase | - |
Pseudomonas aeruginosa |
| 1,6-anhydro-N-acetylmuramic acid kinase | - |
Escherichia coli |
| AnmK | - |
Pseudomonas aeruginosa |
| AnmK | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7000 | - |
1,6-anhydro-N-acetyl-beta-muramate | pH and temperature not specified in the publication | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10 | - |
- |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Pseudomonas aeruginosa | |
| ATP | - |
Escherichia coli | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.4 | - |
ADP | pH and temperature not specified in the publication | Pseudomonas aeruginosa | |
| 0.4 | - |
ADP | pH and temperature not specified in the publication | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Pseudomonas aeruginosa |
| 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 | Escherichia coli |
| 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 | Escherichia coli |
| 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 | Pseudomonas aeruginosa |
| physiological function | enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic | Pseudomonas aeruginosa |
| physiological function | enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic | Escherichia coli |
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