| Entry |
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| Name |
hydroxyquinol 1,2-dioxygenase;
hydroxyquinol dioxygenase;
benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing);
benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)
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| Class |
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
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| Sysname |
hydroxyquinol:oxygen 1,2-oxidoreductase (ring-opening)
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| Reaction(IUBMB) |
hydroxyquinol + O2 = maleylacetate [RN: R04061]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
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| History |
EC 1.13.11.37 created 1989, modified 2013
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| Pathway |
| ec00361 | Chlorocyclohexane and chlorobenzene degradation |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K04098 | hydroxyquinol 1,2-dioxygenase |
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| Genes |
» show all
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| Reference |
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| Authors |
Sze IS, Dagley S. |
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| Title |
Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. |
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| Journal |
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| Reference |
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| Authors |
Ferraroni M, Seifert J, Travkin VM, Thiel M, Kaschabek S, Scozzafava A, Golovleva L, Schlomann M, Briganti F |
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| Title |
Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Hatta T, Nakano O, Imai N, Takizawa N, Kiyohara H |
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| Title |
Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. |
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| Journal |
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| Other DBs |
| UM-BBD (Biocatalysis/Biodegradation Database): | 1.13.11.37 |
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| LinkDB |
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