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

¹ Gut Health Division, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
² Scientific Support Division, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK

Correspondence
Petra Louis
p.louis{at}rowett.ac.uk

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.

The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are: Roseburia sp. A2-183 CoA-transferase, AY796317; Eu. hallii L2-7 CoA-transferase, DQ072258; F. prausnitzii A2-165 CoA-transferase, DQ072259; A. caccae L1-92 CoA-transferase I, DQ151450; A. caccae L1-92 4-hydroxybutyrate dehydrogenase and CoA-transferase II, DQ151451.

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