The Enzyme Database

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Accepted name: propionate kinase
Reaction: ATP + propanoate = ADP + propanoyl phosphate
Other name(s): PduW; TdcD; propionate/acetate kinase
Systematic name: ATP:propanoate phosphotransferase
Comments: Requires Mg2+. Acetate can also act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC, acetate kinase, play important roles in the production of propanoate [1].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 39369-28-3
1.  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]
2.  Palacios, S., Starai, V.J. and Escalante-Semerena, J.C. Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol. J. Bacteriol. 185 (2003) 2802–2810. [DOI] [PMID: 12700259]
3.  Wei, Y. and Miller, C.G. Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium. J. Bacteriol. 181 (1999) 6092–6097. [PMID: 10498722]
4.  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]
5.  Simanshu, D.K. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61 (2005) 52–55. [DOI] [PMID: 16508089]
6.  Simanshu, D.K., Savithri, H.S. and Murthy, M.R. Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily. J. Mol. Biol. 352 (2005) 876–892. [DOI] [PMID: 16139298]
[EC created 2005]

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