L,L-diaminopimelate aminotransferase

In enzymology, a L,L-diaminopimelate aminotransferase (EC 2.6.1.83) is an enzyme that catalyzes the chemical reaction

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

L,L-diaminopimelate aminotransferase
Identifiers
EC no.	2.6.1.83
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 2Z1Z and 2Z20.