BRENDA - Enzyme Database
show all sequences of 1.13.11.36

A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986

Muller, R.; Schmitt, S.; Lingens, F.; Eur. J. Biochem. 125, 579-584 (1982) View publication on PubMed

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ascorbate
protects against autooxidation
Phenylobacterium immobile
Crystallization (Commentary)
Crystallization (Commentary)
Organism
with 37% ammonium sulfate
Phenylobacterium immobile
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for activity
Phenylobacterium immobile
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
Phenylobacterium immobile
-
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Phenylobacterium immobile
-
DSM 1986
-
Oxidation Stability
Oxidation Stability
Organism
inactivated by oxygen, can be reactivated by Fe2+ or ascorbate, Fe2+ much more effective in reactivation
Phenylobacterium immobile
Storage Stability
Storage Stability
Organism
-20°C, stable for months
Phenylobacterium immobile
4°C, crystal suspensions stable for several weeks
Phenylobacterium immobile
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
-
439433
Phenylobacterium immobile
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
-
-
-
?
catechol + O2
-
439433
Phenylobacterium immobile
2-hydroxymuconic acid semialdehyde
-
439433
Phenylobacterium immobile
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.3
-
catechol
-
Phenylobacterium immobile
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ascorbate
protects against autooxidation
Phenylobacterium immobile
Crystallization (Commentary) (protein specific)
Crystallization
Organism
with 37% ammonium sulfate
Phenylobacterium immobile
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for activity
Phenylobacterium immobile
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
Phenylobacterium immobile
-
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
-
-
?
Oxidation Stability (protein specific)
Oxidation Stability
Organism
inactivated by oxygen, can be reactivated by Fe2+ or ascorbate, Fe2+ much more effective in reactivation
Phenylobacterium immobile
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, stable for months
Phenylobacterium immobile
4°C, crystal suspensions stable for several weeks
Phenylobacterium immobile
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2
-
439433
Phenylobacterium immobile
5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
-
-
-
?
catechol + O2
-
439433
Phenylobacterium immobile
2-hydroxymuconic acid semialdehyde
-
439433
Phenylobacterium immobile
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.3
-
catechol
-
Phenylobacterium immobile
Other publictions for EC 1.13.11.36
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
439434
Schmitt
-
One-step purification of chlor ...
Phenylobacterium immobile
J. Immunol. Methods
68
263-267
1984
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
1
-
1
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1
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439435
Schmitt
Chloridazon-catechol dioxygena ...
Phenylobacterium immobile, Phenylobacterium sp.
Hoppe-Seyler's Z. Physiol. Chem.
365
143-150
1984
-
-
-
-
-
-
-
-
-
2
-
2
-
6
-
-
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439433
Muller
A novel non-heme iron-containi ...
Phenylobacterium immobile
Eur. J. Biochem.
125
579-584
1982
1
-
-
1
-
-
-
-
-
1
-
1
-
5
1
-
-
-
-
-
-
2
2
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
2
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
439432
Muller
Catechol 2,3-dioxygenase from ...
Phenylobacterium immobile
Hoppe-Seyler's Z. Physiol. Chem.
358
797-805
1977
-
-
-
-
-
1
1
4
-
3
3
1
-
1
-
-
1
-
-
-
-
1
5
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
4
-
3
3
1
-
-
-
1
-
-
-
1
5
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-