Phenylalanine ammonia-lyase

phenylalanine ammonia-lyase
Identifiers
EC number	4.3.1.24
CAS number	9024-28-6
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
Search PMC articles PubMed articles

In enzymology, a phenylalanine ammonia-lyase (EC 4.3.1.24) 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-cinnamic acid and ammonia.

This enzyme belongs to the family of lyases, to be specific ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-phenylalanine ammonia-lyase (trans-cinnamate-forming). Previously, it was designated EC 4.3.1.5, but that class has been redesignated as EC 4.3.1.24 (phenylalanine ammonia-lyases), EC 4.3.1.25 (tyrosine ammonia-lyases), and EC 4.3.1.26 (phenylalanine/tyrosine ammonia-lyases). 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.

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.

References

• KOUKOL J, CONN EE (1961). "The metabolism of aromatic compounds in higher plants. IV Purification and properties of the phenylalanine deaminase of Hordeum vulgare" (PDF). J. Biol. Chem. 236 (10): 2692–8. PMID 14458851. http://www.jbc.org/content/236/10/2692.full.pdf. Retrieved November 25, 2010. 
• Young MR and Neish AC (1966). "Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum". Phytochemistry 5 (6): 1121–1132. doi:10.1016/S0031-9422(00)86105-1.