Tyrosine phenol-lyase

From Wikipedia, the free encyclopedia

In enzymology, a tyrosine phenol-lyase (EC 4.1.99.2) is an enzyme that catalyzes the chemical reaction

L-tyrosine + H₂O $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 4.1.99.2
BRENDA references for 4.1.99.2 (Recommended.)
PubMed references for 4.1.99.2
PubMed Central references for 4.1.99.2
Google Scholar references for 4.1.99.2
Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K (1970). "Tyrosine phenol lyase. I. Purification, crystallization, and properties". J. Biol. Chem. 245: 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: 1773–7. PMID 4908869.