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 |
Enzyme Information
| 4.1.99.1 |
Tryptophanase.
based on mapping to UniProt P28796
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)
| P28796 |
TNAA_PROVU
Proteus vulgaris
Tryptophanase
|
PDB Structure
| PDB | 1AX4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of tryptophanase.
J.Mol.Biol.
|
