CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
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
J.Mol.Biol.
|