| Type: | Domain | Name: | CoA-transferase family III domain |
| Description: | CoA-transferases are found in organisms from all kingdoms of life. They catalyse reversible transfer reactions of coenzyme A groups from CoA-thioesters to free acids. There are at least three families of CoA-transferases, which differ in sequence and reaction mechanism:Family I consists of CoA-transferases for 3-oxoacids (, ), short-chain fatty acids (, ) and glutaconate (). Most use succinyl-CoA or acetyl-CoA as CoA donors.Family II consists of the homodimeric alpha-subunits of citrate lyase and citramalate lyase (, ). These enzymes catalyse the transfer of acyl carrier protein (ACP) with a covalently bound CoA derivative, but can accept free CoA thioesters as well.Family III consists of formyl-CoA:oxalate CoA-transferase [], succinyl-CoA:(R)-benzylsuccinate CoA-transferase [], (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase [], and butyrobetainyl-CoA:(R)-carnitine CoA-transferase []. These CoA-transferases occur in prokaryotes and eukaryotes, and catalyse CoA-transfer reactions in a highly substrate- and stereo-specific manner [].This entry represents the structural domain of family III CoA-transferases. | Short Name: | CoA-Trfase_III_dom |
