BRENDA - Enzyme Database
show all sequences of 1.13.11.19

Nonheme iron dioxygenase

Nozaki, M.; Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York , 135-165 (1974)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
hydroxylamine
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Se
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Sulfide
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
sulfur
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Inhibitors
Inhibitors
Commentary
Organism
Structure
S
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Se
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Sulfide
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
a non-heme-iron protein, contains 1 g-atom of iron per mol of enzyme (based on a MW of 83000), nearly all of the iron is in the ferric state
Equus caballus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000 SDS-PAGE
Equus caballus
100000
-
method not mentioned
Equus caballus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Equus caballus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Equus caballus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Equus caballus
-
Storage Stability
Storage Stability
Organism
0°C, 70% saturated ammonium sulfate, stable for months
Equus caballus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cysteamine + O2
-
396333
Equus caballus
hypotaurine
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 50000 SDS-PAGE
Equus caballus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
hydroxylamine
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Se
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Sulfide
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
sulfur
cofactor-like compound; sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
S
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Se
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Sulfide
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Equus caballus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
a non-heme-iron protein, contains 1 g-atom of iron per mol of enzyme (based on a MW of 83000), nearly all of the iron is in the ferric state
Equus caballus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000 SDS-PAGE
Equus caballus
100000
-
method not mentioned
Equus caballus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Equus caballus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Equus caballus
-
Storage Stability (protein specific)
Storage Stability
Organism
0°C, 70% saturated ammonium sulfate, stable for months
Equus caballus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cysteamine + O2
-
396333
Equus caballus
hypotaurine
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 50000 SDS-PAGE
Equus caballus
Other publictions for EC 1.13.11.19
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
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)
743204
Liu
Taurine biosynthesis in a fis ...
Danio rerio, Danio rerio ATCC CRL-2643
Mar. Drugs
15
147-161
2017
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1
1
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1
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710836
Stipanuk
Thiol dioxygenases: unique fam ...
Homo sapiens, Mus musculus
Amino Acids
41
91-102
2011
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2
2
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687595
Dominy
Discovery and characterization ...
Mus musculus
J. Biol. Chem.
282
25189-25198
2007
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671185
Coloso Relicardo
Cysteamine dioxygenase: eviden ...
Mus musculus, Rattus norvegicus
Adv. Exp. Med. Biol.
583
25-36
2006
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1
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7
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396418
Kataoka
-
Distribution of cysteamine oxy ...
Bos taurus, Canis lupus familiaris, Equus caballus, Gallus gallus, Mus musculus, octopus, Oryctolagus cuniculus, Rattus norvegicus, Scombridae, Sepiidae, Sus scrofa
Agric. Biol. Chem.
52
1611-1613
1988
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11
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11
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80
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33
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11
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80
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33
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396408
Richerson
Cysteamine dioxygenase ...
Sus scrofa
Methods Enzymol.
143
410-415
1987
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4
2
1
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1
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1
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1
1
1
3
1
1
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1
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396409
Duffel
Selenocysteine ...
Equus caballus, Sus scrofa
Methods Enzymol.
143
148-155
1987
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396411
Cavallini
The specificity of cysteamine ...
Equus caballus
FEBS Lett.
56
348-351
1975
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396333
Nozaki
-
Nonheme iron dioxygenase ...
Equus caballus
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
135-165
1974
4
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396410
Cavallini
-
Cysteamine oxygenase (horse ki ...
Equus caballus
Methods Enzymol.
17B
479-483
1971
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396412
Rotilio
An electron paramagnetic reson ...
Equus caballus
J. Biol. Chem.
245
6235-6239
1970
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396413
Cavallini
Molecular weight of native and ...
Equus caballus
Eur. J. Biochem.
16
537-540
1970
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3
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396414
Cavallini
Interaction of cysteamine oxyg ...
Equus caballus
Eur. J. Biochem.
11
360-363
1969
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396415
Cavallini
Metal content of cysteamine ox ...
Equus caballus
Eur. J. Biochem.
4
209-212
1968
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7
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396416
Wood
Enzymic oxidation of cysteamin ...
Equus caballus
Arch. Biochem. Biophys.
119
368-372
1967
6
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396417
Cavallini
The enzymatic oxidation of cys ...
Equus caballus
J. Biol. Chem.
241
3189-3196
1966
5
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