O-pyrocatechuate decarboxylase
| o-pyrocatechuate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.46 | ||||||||
| CAS number | 37289-48-8 | ||||||||
| 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, an o-pyrocatechuate decarboxylase (EC 4.1.1.46) is an enzyme that catalyzes the chemical reaction
- 2,3-dihydroxybenzoate catechol + CO2
Hence, this enzyme has one substrate, 2,3-dihydroxybenzoate, and two products, catechol 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 2,3-dihydroxybenzoate carboxy-lyase (catechol-forming). This enzyme is also called 2,3-dihydroxybenzoate carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation and carbazole degradation.
References
- Rao PV, Moore K, Towers GH (1967). "O-pyrocatechiuc acid carboxy-lyase from Aspergillus niger". Arch. Biochem. Biophys. 122 (2): 466&ndash, 73. doi:10.1016/0003-9861(67)90220-2. PMID 6066253.
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