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 | Tyrosine phenol-lyase |
Enzyme Information
| 4.1.99.2 |
Tyrosine phenol-lyase.
based on mapping to UniProt P31013
L-tyrosine + H(2)O = phenol + pyruvate + NH(3).
-!- The enzyme cleaves a carbon-carbon bond, releasing phenol 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. -!- The enzyme also slowly catalyzes similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.
|
UniProtKB Entries (1)
| P31013 |
TPL_CITFR
Citrobacter freundii
Tyrosine phenol-lyase
|
PDB Structure
| PDB | 2EZ2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
Biochemistry
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