Tyrosine decarboxylase
Enzyme
| tyrosine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.25 | ||||||||
| CAS no. | 9002-09-9 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
The enzyme tyrosine decarboxylase (EC 4.1.1.25) catalyzes the chemical reaction
- L-tyrosine tyramine + CO2
Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide.
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-tyrosine carboxy-lyase (tyramine-forming). Other names in common use include L-tyrosine decarboxylase, L-(−)-tyrosine apodecarboxylase, and L-tyrosine carboxy-lyase. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
- McGilvery RW, Cohen PP (July 1948). "The decarboxylation of L-phenylalanine by Streptococcus faecalis R". The Journal of Biological Chemistry. 174 (3): 813–6. PMID 18871240.
- v
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Portal:
Biology
