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Phenylalanine decarboxylase

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phenylalanine decarboxylase
Identifiers
EC no.4.1.1.53
CAS no.9075-72-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a phenylalanine decarboxylase (EC 4.1.1.53) is an enzyme that catalyzes the chemical reaction

L-phenylalanine phenethylamine + CO2

Hence, this enzyme has one substrate, L-phenylalanine, and two products, phenethylamine and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use include L-phenylalanine decarboxylase, aromatic L-amino acid decarboxylase, and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal phosphate.

References

  • Lovenberg W, Weissbach H, Udenfriend S (1962). "Aromatic L-amino acid decarboxylase". J. Biol. Chem. 237: 89–93. PMID 14466899.
  • Schulz AR, Oliner L (1967). "The possible role of thyroid aromatic amino acid decarboxylase in thyroxine biosynthesis". Life Sci. 6 (8): 873–80. doi:10.1016/0024-3205(67)90291-3. PMID 6034195.