Biology:Propionate kinase

From HandWiki
Propionate kinase
Identifiers
EC number2.7.2.15
CAS number39369-28-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP + propanoyl phosphate

This enzyme requires Mg2+.

References

  1. "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate". Molecular Microbiology 27 (2): 477–92. January 1998. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901. 
  2. "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". Journal of Bacteriology 185 (9): 2802–10. May 2003. doi:10.1128/jb.185.9.2802-2810.2003. PMID 12700259. 
  3. "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium". Journal of Bacteriology 181 (19): 6092–7. October 1999. PMID 10498722. 
  4. "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". Journal of Bacteriology 187 (7): 2386–94. April 2005. doi:10.1128/jb.187.7.2386-2394.2005. PMID 15774882. 
  5. "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium". Acta Crystallographica Section F 61 (Pt 1): 52–5. January 2005. doi:10.1107/s1744309104026429. PMID 16508089. 
  6. "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". Journal of Molecular Biology 352 (4): 876–92. September 2005. doi:10.1016/j.jmb.2005.07.069. PMID 16139298. 

External links