| valine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.14 | ||||||||
| CAS no. | 9031-16-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a valine decarboxylase (EC 4.1.1.14) is an enzyme that catalyzes the chemical reaction
- L-valine 2-methylpropanamine + CO2
Hence, this enzyme has one substrate, L-valine, and two products, 2-methylpropanamine 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-valine carboxy-lyase (2-methylpropanamine-forming). Other names in common use include leucine decarboxylase and L-valine carboxy-lyase. It employs one cofactor, pyridoxal phosphate.
References
- Sutton CR, King HK (February 1962). "Inhibition of leucine decarboxylase by thiol-binding reagents". Archives of Biochemistry and Biophysics. 96 (2): 360–70. doi:10.1016/0003-9861(62)90421-6. PMID 13918558.
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