succinyltransferase

Succinyltransferases are a group of acyltransferase enzymes that catalyze the transfer of a succinyl group from succinyl-CoA to an acceptor molecule, producing CoA and a succinylated product. The reaction is generally described as succinyl-CoA plus an acceptor → CoA plus the succinylated derivative of the acceptor. This chemistry enables the formation of N-succinyl or O-succinyl derivatives that serve as intermediates in various biosynthetic pathways.

Many characterized succinyltransferases act on amino substrates, transferring the succinyl group to amine or hydroxyl groups. Well-studied examples include ornithine N-succinyltransferase, which participates in arginine biosynthesis, and tetrahydrodipicolinate N-succinyltransferase (DapD), a key enzyme in a lysine biosynthesis route used by several bacteria. Other family members act on different acceptors within central metabolism, reflecting a broader role in channeling succinyl-CoA into specific biosynthetic intermediates. Succinyltransferases are primarily found in bacteria and some archaea, reflecting the prominence of succinylated intermediates in microbial amino acid pathways.

Structural and biochemical studies indicate that succinyltransferases comprise diverse sequences yet share the core function of binding succinyl-CoA and a suitable acceptor, often operating through a conserved acyl-transfer mechanism. Their activity can be influenced by cellular levels of succinyl-CoA and CoA, linking succinylation steps to metabolic state.

In summary, succinyltransferases catalyze the formation of succinylated metabolites that are important in bacterial amino acid biosynthesis and metabolism, with notable representatives such as ornithine N-succinyltransferase and DapD illustrating their role in arginine and lysine pathways.