Hydroxyquinol 1,2-dioxygenase
| Hydroxyquinol 1,2-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.37 | ||||||||
| CAS no. | 91847-14-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Hydroxyquinol 1,2-dioxygenase (EC 1.13.11.37) is an enzyme isolated from Trichosporon cutaneum that catalyzes the chemical reaction
The two substrates of this enzyme are hydroxyquinol and oxygen. Its product is 3-hydroxy-cis,cis-muconic acid.[1][2]
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, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1TMX.
References
- ↑ Enzyme 1.13.11.37 at KEGG Pathway Database.
- ↑ Sze, I. S.; Dagley, S. (1984). "Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum". Journal of Bacteriology. 159 (1): 353–359. doi:10.1128/JB.159.1.353-359.1984. PMC 215637. PMID 6539772.