Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
In enzymology, a phenylalanine ammonia-lyase (EC number|4.3.1.5) is an enzyme that catalyzes the chemical reaction
:L-phenylalanine 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.
tructural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1T6J, PDB link|1T6P, PDB link|1W27, PDB link|1Y2M, and PDB link|2NYF.
References
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External links
::"The CAS registry number for this enzyme class is CAS registry|9024-28-6."
Gene Ontology (GO) codes
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