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 | Aspartate aminotransferase |
Enzyme Information
| 2.6.1.1 |
Aspartate transaminase.
based on mapping to UniProt P00509
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.
|
UniProtKB Entries (1)
| P00509 |
AAT_ECOLI
Escherichia coli K-12
Aspartate aminotransferase
|
PDB Structure
| PDB | 1SPA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Biochemistry
|
