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Literature summary extracted from

  • Dai, J.; Qu, H.; Yu, Z.; Yang, J.; Zhang, H.
    Computational analysis of AnmK-like kinase: New insights into the cell wall metabolism of fungi (2015), J. Theor. Biol., 379, 59-65.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.170 gene anmK, phylogenetic analysis and tree Escherichia coli
2.7.1.170 phylogenetic analysis Shewanella oneidensis
2.7.1.232 gene lgk, phylogenetic analysis and tree Lipomyces starkeyi
2.7.1.232 gene lgk, phylogenetic analysis and tree Aspergillus terreus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.170 Mg2+ required Escherichia coli
2.7.1.170 Mg2+ required Shewanella oneidensis
2.7.1.232 Mg2+ required Lipomyces starkeyi
2.7.1.232 Mg2+ required Aspergillus terreus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O Escherichia coli
-
 ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O Shewanella oneidensis
-
 ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O Shewanella oneidensis MR-1 / ATCC 700550
-
 ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.232 ATP + levoglucosan + H2O Lipomyces starkeyi
-
 ADP + D-glucopyranose 6-phosphate
-
 ?
2.7.1.232 ATP + levoglucosan + H2O Aspergillus terreus
-
 ADP + D-glucopyranose 6-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.170 Escherichia coli P77570 gene anmK
-
2.7.1.170 Shewanella oneidensis Q8EHB5 gene anmK
-
2.7.1.170 Shewanella oneidensis MR-1 / ATCC 700550 Q8EHB5 gene anmK
-
2.7.1.232 Aspergillus terreus
-
 gene lgk
-
2.7.1.232 Lipomyces starkeyi
-
 lgk
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate catalytic mechanism, molecular docking, dynamics simulation Escherichia coli
a
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate catalytic mechanism, molecular docking, dynamics simulation Shewanella oneidensis
a
2.7.1.232 ATP + 1,6-anhydro-beta-D-glucopyranose + H2O = ADP + 6-phospho-alpha-D-glucopyranose catalytic mechanism, molecular docking, dynamics simulation Lipomyces starkeyi
a
2.7.1.232 ATP + 1,6-anhydro-beta-D-glucopyranose + H2O = ADP + 6-phospho-alpha-D-glucopyranose catalytic mechanism, molecular docking, dynamics simulation Aspergillus terreus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
-
 Escherichia coli ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
-
 Shewanella oneidensis ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.170 ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
-
 Shewanella oneidensis MR-1 / ATCC 700550 ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
 ?
2.7.1.232 ATP + levoglucosan + H2O
-
 Lipomyces starkeyi ADP + D-glucopyranose 6-phosphate
-
 ?
2.7.1.232 ATP + levoglucosan + H2O
-
 Aspergillus terreus ADP + D-glucopyranose 6-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.170 1,6-anhydro-N-acetylmuramic acid kinase
-
 Escherichia coli
2.7.1.170 1,6-anhydro-N-acetylmuramic acid kinase
-
 Shewanella oneidensis
2.7.1.170 AnmK
-
 Escherichia coli
2.7.1.170 AnmK
-
 Shewanella oneidensis
2.7.1.232 levoglucosan kinase
-
 Lipomyces starkeyi
2.7.1.232 LGK
-
 Lipomyces starkeyi

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.170 ATP
-
 Escherichia coli
2.7.1.170 ATP
-
 Shewanella oneidensis
2.7.1.232 ATP
-
 Lipomyces starkeyi
2.7.1.232 ATP
-
 Aspergillus terreus

General Information

EC Number General Information Comment Organism
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 Escherichia coli
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 Shewanella oneidensis
2.7.1.170 additional information three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview Escherichia coli
2.7.1.232 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 Aspergillus terreus
2.7.1.232 evolution phylogenetic analysis and comparison of levoglucan kinase with 1,6-anhydro-N-acetylmuramic acid 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 Lipomyces starkeyi
2.7.1.232 additional information three dimensional structure analysis, comparison with 1,6-anhydro-N-acetylmuramic acid kinase and AnmK-like enzymes, overview Lipomyces starkeyi