4-carboxymuconolactone decarboxylase
| 4-carboxymuconolactone decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.44 | ||||||||
| CAS no. | 37289-46-6 | ||||||||
| 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 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) catalyzes the chemical reaction
- 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate 4,5-dihydro-5-oxofuran-2-acetate + 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-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming). Other names in common use include gamma-4-carboxymuconolactone decarboxylase,[citation needed] and 4-carboxymuconolactone carboxy-lyase.[citation needed] This enzyme participates in benzoate degradation via hydroxylation.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2AF7.
References[edit]
- Ornston LN (August 1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway". The Journal of Biological Chemistry. 241 (16): 3795–9. PMID 5330966.
- Ornston LN (1970). "Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549. doi:10.1016/0076-6879(71)17237-0.
