LL-diaminopimelate aminotransferase

In enzymology, a LL-diaminopimelate aminotransferase is an enzyme that catalyzes the chemical reaction


 * LL-2,6-diaminoheptanedioate + 2-oxoglutarate $$\rightleftharpoons$$ (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O

Thus, the two substrates of this enzyme are LL-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its 3 products are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, L-glutamate, and H2O.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT. This enzyme participates in lysine biosynthesis.

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