enzymology An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...

, a 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase () is an

enzyme An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...

that catalyzes the

chemical reaction A chemical reaction is a process that leads to the chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, ...

:succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H₂O

\rightleftharpoons

CoA + N-succinyl-L-2-amino-6-oxoheptanedioate The 3 substrates of this enzyme are succinyl-CoA, (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and H₂O, whereas its two products are CoA and N-succinyl-L-2-amino-6-oxoheptanedioate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The

systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ...

of this enzyme class is succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Other names in common use include tetrahydropicolinate succinylase, tetrahydrodipicolinate N-succinyltransferase, tetrahydrodipicolinate succinyltransferase, succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase, succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and N-succinyltransferase. This enzyme participates in lysine biosynthesis.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .

References

* EC 2.3.1 Enzymes of known structure {{2.3-enzyme-stub