In enzymology, a muconolactone Δ-isomerase (EC 5.3.3.4) is an enzyme that catalyzes the chemical reaction
| Muconolactone Δ-isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.3.3.4 | ||||||||
| CAS no. | 37318-46-0 | ||||||||
| 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 | ||||||||
| |||||||||
- (S)-5-oxo-2,5-dihydrofuran-2-acetate 5-oxo-4,5-dihydrofuran-2-acetate
Hence, this enzyme has one substrate, (S)-5-oxo-2,5-dihydrofuran-2-acetate, and one product, 5-oxo-4,5-dihydrofuran-2-acetate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 5-oxo-4,5-dihydrofuran-2-acetate Delta3-Delta2-isomerase. This enzyme is also called muconolactone isomerase. 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 1MLI.
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.
