Propionate kinase

Propionate kinase
Identifiers
EC number 2.7.2.15
CAS number 39369-28-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Propionate kinase (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

ATP + propanoate \rightleftharpoons ADP + propanoyl phosphate

This enzyme requires Mg2+.

References

  1. Heßlinger, C., Fairhurst, S.A. and Sawers, G. (1998). "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. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.
  2. Palacios, S., Starai, V.J. and Escalante-Semerena, J.C. (2003). "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. doi:10.1128/jb.185.9.2802-2810.2003. PMID 12700259.
  3. Wei, Y. and Miller, C.G. (1999). "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium". J. Bacteriol. 181: 6092–6097. PMID 10498722.
  4. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. (2005). "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". J. Bacteriol. 187: 2386–2394. doi:10.1128/jb.187.7.2386-2394.2005. PMID 15774882.
  5. Simanshu, D.K. (2005). "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. doi:10.1107/s1744309104026429. PMID 16508089.
  6. Simanshu, D.K., Savithri, H.S. and Murthy, M.R. (2005). "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. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.

External links

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