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 / EGO | ||||||
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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): 1767–72. PMID 4908868.
- Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K (1970). "Tyrosine phenol lyase. II. Cofactor requrements". J. Biol. Chem. 245 (7): 1773–7. PMID 4908869.