EC 2.7.2.1 - Acetate kinase

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IntEnz Enzyme Nomenclature
EC 2.7.2.1

Names

Accepted name:
acetate kinase
Other names:
acetokinase
AckA
AK
acetic kinase
acetate kinase (phosphorylating)
Systematic name:
ATP:acetate phosphotransferase

Reaction

Cofactor

Comments:

Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00826
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008776
CAS Registry Number: 9027-42-3
UniProtKB/Swiss-Prot: (347) [show] [UniProt]

References

  1. Romain, Y., Demassieux, S. and Carriere, S.
    Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines.
    Biochem. Biophys. Res. Commun. 106: 999-1005 (1982). [PMID: 6956338]
  2. Romano, A.H. and Nickerson, W.J.
    Cystine reductase of pea seeds and yeasts.
    J. Biol. Chem. 208: 409-416 (1954). [PMID: 13174550]
  3. Stern, J.R. and Ochoa, S.
    Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes.
    J. Biol. Chem. 191: 161-172 (1951). [PMID: 14850456]
  4. Fox, D.K. and Roseman, S.
    Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli.
    J. Biol. Chem. 261: 13487-13497 (1986). [PMID: 3020034]
  5. Knorr, R., Ehrmann, M.A. and Vogel, R.F.
    Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis.
    Microbiol. Res. 156: 267-277 (2001). [PMID: 11716215]
  6. Buss, K.A., Cooper, D.R., Ingram-Smith, C., Ferry, J.G., Sanders, D.A. and Hasson, M.S.
    Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.
    J. Bacteriol. 183: 680-686 (2001). [PMID: 11133963]
  7. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G.
    Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase.
    J. Bacteriol. 187: 2386-2394 (2005). [PMID: 15774882]
  8. Gorrell, A., Lawrence, S.H. and Ferry, J.G.
    Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.
    J. Biol. Chem. 280: 10731-10742 (2005). [PMID: 15647264]
  9. Heßlinger, C., Fairhurst, S.A. and Sawers, G.
    Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate.
    Mol. Microbiol. 27: 477-492 (1998). [PMID: 9484901]

[EC 2.7.2.1 created 1961, modified 2005]