| EC |
1.13.11.36 |
| Accepted name: |
chloridazon-catechol dioxygenase |
| Reaction: |
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone |
| Other name(s): |
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing) |
| Systematic name: |
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (ring-opening) |
| Comments: |
An iron protein, requiring additional Fe2+. Not identical with EC 1.13.11.1 (catechol 1,2-dioxygenase), EC 1.13.11.2 (catechol 2,3-dioxygenase) or EC 1.13.11.5 (homogentisate 1,2-dioxygenase). Involved in the breakdown of the herbicide chloridazon. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82869-32-7 |
| References: |
| 1. |
Müller, R, Haug, S., Eberspächer, J. and Lingens, F. Catechol-2,3-Dioxygenase aus Pyrazon-abbauenden Bakterien. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 797–805. [PMID: 19349] |
| 2. |
Müller, R., Schmitt, S. and Lingens, F. A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986. Eur. J. Biochem. 125 (1982) 579–584. [DOI] [PMID: 6811270] |
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| [EC 1.13.11.36 created 1984] |
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