InterPro: IPR003673 CoA-transferase family III

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 (EC:2.8.3.5, EC:2.8.3.6), short-chain fatty acids (EC:2.8.3.8, EC:2.8.3.9) and glutaconate (EC:2.8.3.12). Most use succinyl-CoA or acetyl-CoA as CoA donors.
• Family II consists of the homodimeric alpha-subunits of citrate lyase and citramalate lyase (EC:2.8.3.10, EC:2.8.3.11). 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 [1], succinyl-CoA:(R)-benzylsuccinate CoA-transferase [2], (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase [3], and butyrobetainyl-CoA:(R)-carnitine CoA-transferase [4]. These CoA-transferases occur in prokaryotes and eukaryotes, and catalyse CoA-transfer reactions in a highly substrate- and stereo-specific manner [5].

This entry represents family III CoA-transferases.