| hydroxyquinol 1,2-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.37 | ||||||||
| CAS no. | 91847-14-2 | ||||||||
| 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 hydroxyquinol 1,2-dioxygenase (EC 1.13.11.37) is an enzyme that catalyzes the chemical reaction
- benzene-1,2,4-triol + O2 3-hydroxy-cis,cis-muconate
Thus, the two substrates of this enzyme are benzene-1,2,4-triol (hydroxyquinol) and O2, whereas its product is 3-hydroxy-cis,cis-muconate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing). This enzyme is also called hydroxyquinol dioxygenase. This enzyme participates in benzoate degradation via hydroxylation and 1,4-dichlorobenzene degradation. It employs one cofactor, iron.
Structural studies
As of late 2007[update], only one structure has been solved for this class of enzymes, with the PDB accession code 1TMX.
References
- Sze IS, Dagley S (1984). "Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum". J. Bacteriol. 159 (1): 353–9. doi:10.1128/JB.159.1.353-359.1984. PMC 215637. PMID 6539772.
This page was last edited on 26 August 2023, at 14:31