The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase

Microbiology (Reading). 1999 Jun;145 ( Pt 6):1381-1388. doi: 10.1099/13500872-145-6-1381.


Biochemical and genetic evidence is presented to demonstrate that the prpE gene of Salmonella typhimurium encodes propionyl-CoA synthetase, an enzyme required for the catabolism of propionate in this bacterium. While prpE mutants used propionate as carbon and energy source, prpE mutants that lacked acetyl-CoA synthetase (encoded by acs) did not, indicating that Acs can compensate for the lack of PrpE in prpE mutants. Cell-free extracts enriched for PrpE catalysed the formation of propionyl-CoA in a propionate-, ATP-, Mg2+- and HS-CoA dependent manner. Acetate substituted for propionate in the reaction at 48% the rate of propionate; butyrate was not a substrate for PrpE. The propionyl-CoA synthetase activity of PrpE was specific for ATP. GTP, ITP, CTP and TTP were not used as substrates by the enzyme. UV-visible spectrophotometry, HPLC and MS data demonstrated that propionyl-CoA was the product of the reaction catalysed by PrpE.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromatography, High Pressure Liquid
  • Coenzyme A Ligases / genetics*
  • Coenzyme A Ligases / metabolism
  • Genes, Bacterial
  • Mass Spectrometry
  • Mutation
  • Operon
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Salmonella typhimurium / enzymology
  • Salmonella typhimurium / genetics*


  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Coenzyme A Ligases
  • propionate - CoA ligase
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase

Associated data

  • GENBANK/U51879