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Literature summary for 2.7.2.1 extracted from

  • Asgari, S.; Shariati, P.; Ebrahim-Habibi, A.
    Targeting acetate kinase: inhibitors as potential bacteriostatics (2013), J. Microbiol. Biotechnol., 23, 1544-1553.
    View publication on PubMed
Search for more literature for 2.7.2.1

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibitor design using the the structure of the catalytic intermediate Escherichia coli
trifluoroethanol leads to reduced growth and acetate content, binding mode by molecular docking Escherichia coli
trifluoroethyl butyrate leads to reduced growth and acetate content, binding mode by molecular docking Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate Escherichia coli
-
 ADP + acetyl phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6A3 PTCC 1399
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate
-
 Escherichia coli ADP + acetyl phosphate
-
 r

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Escherichia coli
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information construction of the three-dimensional structure of the Escherichia coli acetate kinase by use of molecular homology modeling using the structure of the enzyme from Thermotoga maritima, overview Escherichia coli