Muconolactone Δ-isomerase
| 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 | ||||||||
| |||||||||
In enzymology, a muconolactone Δ-isomerase (EC 5.3.3.4) is an enzyme that catalyzes the chemical reaction
- (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
[edit]As 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.
