Phenylalanine decarboxylase
| phenylalanine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC number | 4.1.1.53 | ||||||||
| CAS number | 9075-72-3 | ||||||||
| 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 | ||||||||
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In enzymology, a phenylalanine decarboxylase (EC 4.1.1.53) is an enzyme that catalyzes the chemical reaction
- L-phenylalanine phenylethylamine + CO2
Hence, this enzyme has one substrate, L-phenylalanine, and two products, phenylethylamine 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.
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