CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family | Aspartate aminotransferase |
Enzyme Information
| 2.6.1.1 |
Aspartate transaminase.
based on mapping to UniProt P00508
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
|
| 2.6.1.7 |
Kynurenine--oxoglutarate transaminase.
based on mapping to UniProt P00508
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
-!- Also acts on 3-hydroxykynurenine. -!- The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
|
UniProtKB Entries (1)
| P00508 |
AATM_CHICK
Gallus gallus
Aspartate aminotransferase, mitochondrial
|
PDB Structure
| PDB | 1AKC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Biochemistry
|