The enzyme tyrosine phenol-lyase (EC 4.1.99.2) catalyzes the chemical reaction
| tyrosine phenol-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.99.2 | ||||||||
| CAS no. | 9059-31-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- L-tyrosine + H2O phenol + pyruvate + NH3
This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tyrosine phenol-lyase (deaminating; pyruvate-forming). Other names in common use include beta-tyrosinase, and L-tyrosine phenol-lyase (deaminating). This enzyme participates in tyrosine metabolism and nitrogen metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
editAs of late 2007, five structures have been solved for this class of enzyme, with PDB accession codes 1C7G, 1TPL, 2EZ1, 2EZ2, and 2TPL.
References
edit- Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K (1970). "Tyrosine phenol lyase. I. Purification, crystallization, and properties". J. Biol. Chem. 245 (7): 1767–72. doi:10.1016/S0021-9258(19)77158-0. PMID 4908868.
- Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K (1970). "Tyrosine phenol lyase. II. Cofactor requirements". J. Biol. Chem. 245 (7): 1773–7. doi:10.1016/S0021-9258(19)77159-2. PMID 4908869.
