The enzyme 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- 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
editAs 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. doi:10.1016/S0021-9258(18)99841-8. PMID 5330966.
- Ornston LN (1970). "Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida)". Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida). Methods Enzymol. Vol. 17A. pp. 529–549. doi:10.1016/0076-6879(71)17237-0. ISBN 978-0-12-181874-6.
