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

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