The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase.
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.
Alexander R
AR
Horswill
Jorge C
JC
Escalante-Semerena
D002851:Chromatography, High Pressure Liquid; D003066:Coenzyme A Ligases / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D013058:Mass Spectrometry; D009154:Mutation; D009876:Operon; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012486:Salmonella typhimurium / Q000201:enzymology / Q000235:genetics*; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D003066:Coenzyme A Ligases; C068072:propionate - CoA ligase; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase