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 | Tryptophanase |
Enzyme Information
| 4.1.99.1 |
Tryptophanase.
based on mapping to UniProt P0A853
L-tryptophan + H(2)O = indole + pyruvate + NH(3).
-!- The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids.
|
UniProtKB Entries (1)
| P0A853 |
TNAA_ECOLI
Escherichia coli K-12
Tryptophanase
|
PDB Structure
| PDB | 2V1P |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Conformational Changes and Loose Packing Promote E. Coli Tryptophanase Cold Lability.
Bmc Struct.Biol.
|
