Arylmalonate decarboxylase
In enzymology, an arylmalonate decarboxylase (EC 4.1.1.76) is an enzyme that catalyzes the chemical reaction
- 2-aryl-2-methylmalonate 2-arylpropanoate + CO2
| arylmalonate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.76 | ||||||||
| CAS number | 144713-36-0 | ||||||||
| 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 | ||||||||
| |||||||||
Hence, this enzyme has one substrate, 2-aryl-2-methylmalonate, and two products, 2-arylpropanoate 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 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropanoate-forming). Other names in common use include AMDASE, 2-aryl-2-methylmalonate carboxy-lyase, and 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropionate-forming).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DGD.
References
- Miyamoto K, Ohta H (1992). "Cloning and heterologous expression of a novel arylmalonate decarboxylase gene from Alcaligenes bronchisepticus KU 1201". Appl. Microbiol. Biotechnol. 38 (2): 234–8. doi:10.1007/bf00174474. PMID 1369144. S2CID 11058932.
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