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IUBMB Comments An iron protein, requiring additional Fe2+ 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.
Synonyms
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chloridazoncatechol dioxygenase
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing)
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.
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3-methylpyrocatechol + O2
2-hydroxy-3-methylmuconic acid semialdehyde
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Substrates: -
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4-methylpyrocatechol + O2
2-hydroxy-3-methylmuconic acid semialdehyde
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Substrates: -
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
catechol + O2
2-hydroxymuconic acid semialdehyde
additional information
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: -
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: enzyme of pyrazone metabolism
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: -
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catechol + O2
2-hydroxymuconic acid semialdehyde
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Substrates: -
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catechol + O2
2-hydroxymuconic acid semialdehyde
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Substrates: -
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additional information
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Substrates: high number of potential substrates tested for activity, low specificity
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additional information
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Substrates: high number of potential substrates tested for activity, low specificity
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: -
?
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: enzyme of pyrazone metabolism
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5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
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Substrates: -
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Co2+
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can partially replace Fe2+
Zn2+
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can partially replace Fe2+
Fe2+
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required for activity
Fe2+
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required for activity
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high ionic strength
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ascorbate
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protects against autooxidation
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0.017
3-Methylpyrocatechol
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0.16
4-Methylpyrocatechol
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0.2
5-Amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone
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DSM 1986
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brenda
various strains
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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200000
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analytical ultracentrifugation
34000
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6 * 34000, SDS-PAGE
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hexamer
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6 * 34000, SDS-PAGE
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with 37% ammonium sulfate
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high osmotic sensitivity
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inactivated by oxygen, can be reactivated by Fe2+ or ascorbate, Fe2+ much more effective in reactivation
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439433
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-20°C, stable for months
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4°C, crystal suspensions stable for several weeks
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Muller, R.; Haug, S.; Eberspcher, J.; Lingens, F.
Catechol 2,3-dioxygenase from pyrazon-degrading bacteria
Hoppe-Seyler's Z. Physiol. Chem.
358
797-805
1977
Phenylobacterium immobile
brenda
Muller, R.; Schmitt, S.; Lingens, F.
A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986
Eur. J. Biochem.
125
579-584
1982
Phenylobacterium immobile
brenda
Schmitt, S.; Muller, R.; Lingens, F.
One-step purification of chloridazon-catechol dioxygenase by immunoaffinity chromatography on thiol-sepharose bound IgG
J. Immunol. Methods
68
263-267
1984
Phenylobacterium immobile
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brenda
Schmitt, S.; Muller, R.; Wegst, W.; Lingens, F.
Chloridazon-catechol dioxygenases, a distinct group of meta-cleaving enzymes
Hoppe-Seyler's Z. Physiol. Chem.
365
143-150
1984
Phenylobacterium immobile, Phenylobacterium sp.
brenda
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