EC 2.7.2.15 - Propionate kinase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.7.2.15

Names

Accepted name:
propionate kinase
Other names:
PduW
TdcD
propionate/acetate kinase
Systematic name:
ATP:propanoate phosphotransferase

Reaction

Cofactor

Comments:

Requires Mg2+. Both propanoate and acetate can act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00826
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008980
UniProtKB/Swiss-Prot: (21) [show] [UniProt]

References

  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: 477-492 (1998). [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: 2802-2810 (2003). [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: 6092-6097 (1999). [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: 2386-2394 (2005). [PMID: 15774882]
  5. Simanshu, D.K. and Murthy M.R.N.
    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: 52-55 (2005).
  6. Simanshu, D.K., Savithri, H.S. and Murthy M.R.N.
    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: 876-892 (2005). [PMID: 16139298]

[EC 2.7.2.15 created 2005]