A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

Cedric Charrier, Gary J. Duncan, Martin D. Reid, Garry J. Rucklidge, Donna Henderson, Pauline Young, Valerie J. Russell, Rustam Irekovitch Aminov, Harry J. Flint, Petra Louis (Corresponding Author)

Research output: Contribution to journalArticlepeer-review

51 Citations (Scopus)
16 Downloads (Pure)


Bacterial butyryl-CoA CoA-transferase activity plays a key role in butyrate formation in the human colon, but the enzyme and corresponding gene responsible for this activity have not previously been identified. A novel CoA-transferase gene is described from the colonic bacterium Roseburia sp. A2-183, with similarity to acetyl-CoA hydrolase as well as 4-hydroxybutyrate CoA-transferase sequences. The gene product, overexpressed in an Escherichia coli lysate, showed activity with butyryl-CoA and to a lesser degree propionyl-CoA in the presence of acetate. Butyrate, propionate, isobutyrate and valerate competed with acetate as the co-substrate. Despite the sequence similarity to 4-hydroxybutyrate CoA-transferases, 4-hydroxybutyrate did not compete with acetate as the co-substrate. Thus the CoA-transferase preferentially uses butyryl-CoA as substrate. Similar genes were identified in other butyrate-producing human gut bacteria from clostridial clusters IV and XIVa, while other candidate CoA-transferases for butyrate formation could not be detected in Roseburia sp. A2-183. This suggests strongly that the newly identified group of CoA-transferases described here plays a key role in butyrate formation in the human colon.

Original languageEnglish
Pages (from-to)179-185
Number of pages7
Issue number1
Publication statusPublished - Jan 2006


  • coenzyme-A-transferase
  • clostridium-acetobutylicum ATCC-824
  • world-wide-web
  • acidaminococcus-fermentans
  • butyrivibrio-fibrisolvens
  • acetate utilization
  • molecular analysis
  • human gut
  • cloning
  • purification

Cite this