| chloridazon-catechol dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.36 | ||||||||
| CAS no. | 82869-32-7 | ||||||||
| 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 | ||||||||
| |||||||||
Chloridazon-catechol dioxygenase ( EC 1.13.11.36) is an enzyme that catalyzes the chemical reaction
- 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
Thus, the two substrates of this enzyme are 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone and oxygen, whereas its product is 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone.
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 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing). It employs one cofactor, iron.
References
- Muller R, Haug S, Eberspacher J, Lingens F (1977). "[Catechol 2,3-dioxygenase from pyrazon-degrading bacteria (author's transl)]". Hoppe-Seyler's Z. Physiol. Chem. 358 (7): 797–805. doi: 10.1515/bchm2.1977.358.2.797. PMID 19349.
- Muller R, Schmitt S, Lingens F (1982). "A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986". Eur. J. Biochem. 125 (3): 579–84. doi: 10.1111/j.1432-1033.1982.tb06722.x. PMID 6811270.
