Phenylalanine decarboxylase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 4.1.1.53
- BRENDA references for 4.1.1.53 (Recommended.)
- PubMed references for 4.1.1.53
- PubMed Central references for 4.1.1.53
- Google Scholar references for 4.1.1.53
- 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: 873–80. doi: . PMID 6034195.
[edit] External links
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- The CAS registry number for this enzyme class is 9075-72-3.