CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family LL-diaminopimelate aminotransferase, chloroplastic

Enzyme Information

2.6.1.83
LL-diaminopimelate aminotransferase.
based on mapping to UniProt Q93ZN9
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5- tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H(2)O.
-!- In vivo, the reaction occurs in the opposite direction to that shown above. -!- This is one of the final steps in the lysine biosynthesis pathway of plants (ranging from mosses to flowering plants). -!- Meso-diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. -!- 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate. -!- It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.

UniProtKB Entries (1)

Q93ZN9
DAPAT_ARATH
Arabidopsis thaliana
LL-diaminopimelate aminotransferase, chloroplastic

PDB Structure

PDB 2Z20
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia
Watanabe, N., Cherney, M.M., van Belkum, M.J., Marcus, S.L., Flegel, M.D., Clay, M.D., Deyholos, M.K., Vederas, J.C., James, M.N.
J.Mol.Biol.