| EC |
1.13.11.37 |
| Accepted name: |
hydroxyquinol 1,2-dioxygenase |
| Reaction: |
hydroxyquinol + O2 = maleylacetate |
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For diagram of 4-nitrophenol metabolism, click here |
| Glossary: |
hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate
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| Other name(s): |
hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing); benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening) |
| Systematic name: |
hydroxyquinol:oxygen 1,2-oxidoreductase (ring-opening) |
| Comments: |
An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 91847-14-2 |
| References: |
| 1. |
Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353–359. [PMID: 6539772] |
| 2. |
Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144–21154. [DOI] [PMID: 15772073] |
| 3. |
Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267–272. [DOI] [PMID: 16232466] |
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| [EC 1.13.11.37 created 1989, modified 2013] |
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