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 | Serine--pyruvate aminotransferase |
Enzyme Information
| 2.6.1.51 |
Serine--pyruvate transaminase.
based on mapping to UniProt P21549
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
-!- The liver enzyme may be identical with EC 2.6.1.44.
|
| 2.6.1.44 |
Alanine--glyoxylate transaminase.
based on mapping to UniProt P21549
L-alanine + glyoxylate = pyruvate + glycine.
-!- With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. -!- A second component also catalyzes the reaction of EC 2.6.1.51.
|
UniProtKB Entries (1)
| P21549 |
SPYA_HUMAN
Homo sapiens
Serine--pyruvate aminotransferase
|
PDB Structure
| PDB | 5OG0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.
Sci Rep
|