ExplorEnz: EC 2.7.2.1

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2.7.2.1

Accepted name:

acetate kinase

Reaction:

ATP + acetate = ADP + acetyl phosphate

Other name(s):

acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating)

Systematic name:

ATP:acetate phosphotransferase

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:

BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-42-3

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 (1982) 999–1005. [DOI] [PMID: 6956338]
2.	Romano, A.H. and Nickerson, W.J. Cystine reductase of pea seeds and yeast. J. Biol. Chem. 208 (1954) 409–416. [PMID: 13174550]
3.	Stern, J.R. and Ochoa, S. Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes. J. Biol. Chem. 191 (1951) 161–172. [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 (1986) 13487–13497. [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 (2001) 267–277. [DOI] [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 (2001) 680–686. [DOI] [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 (2005) 2386–2394. [DOI] [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 (2005) 10731–10742. [DOI] [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 (1998) 477–492. [DOI] [PMID: 9484901]

[EC 2.7.2.1 created 1961, modified 2005]