Phenylalanine ammonia-lyase

From Wikipedia, the free encyclopedia

In enzymology, a phenylalanine ammonia-lyase (EC 4.3.1.5) is an enzyme that catalyzes the chemical reaction

L-phenylalanine $\rightleftharpoons$ trans-cinnamate + NH₃

Hence, this enzyme has one substrate, L-phenylalanine, and two products, trans-cinnamate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-phenylalanine ammonia-lyase (trans-cinnamate-forming). Other names in common use include tyrase, phenylalanine deaminase, tyrosine ammonia-lyase, L-tyrosine ammonia-lyase, phenylalanine ammonium-lyase, PAL, and L-phenylalanine ammonia-lyase. This enzyme participates in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, nitrogen metabolism, phenylpropanoid biosynthesis, and alkaloid biosynthesis ii.

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 1T6J, 1T6P, 1W27, 1Y2M, and 2NYF.

[edit] References

IUBMB entry for 4.3.1.5
BRENDA references for 4.3.1.5 (Recommended.)
PubMed references for 4.3.1.5
PubMed Central references for 4.3.1.5
Google Scholar references for 4.3.1.5
KOUKOL J, CONN EE (1961). "The metabolism of aromatic compounds in higher plans. IV Purification and properties of the phenylalanine deaminase of Hordeum vulgare". J. Biol. Chem. 236: 2692–8. PMID 14458851.
Young MR and Neish AC (1966). "Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum". Phytochemistry 5: 1121–1132. doi:10.1016/S0031-9422(00)86105-1.