Tyrosine phenol-lyase
| tyrosine phenol-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.99.2 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
In enzymology, a tyrosine phenol-lyase (EC 4.1.99.2) is an enzyme that catalyzes the chemical reaction
- L-tyrosine + H2O phenol + pyruvate + NH3
Thus, the two substrates of this enzyme are L-tyrosine and H2O, whereas its 3 products are phenol, pyruvate, and 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
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1C7G, 1TPL, 2EZ1, 2EZ2, and 2TPL.
References
- 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&ndash, 72. 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&ndash, 7. PMID 4908869.