BRENDA - Enzyme Database
show all sequences of 1.13.11.20

Purification and characterization of a cysteine dioxygenase from the yeast phase of Histoplasma capsulatum

Kumar, V.; Maresca, B.; Sacco, M.; Goewert, R.; Kobayashi, G.S.; Medoff, G.; Biochemistry 22, 762-768 (1983)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
NADH
stimulates
Histoplasma capsulatum
General Stability
General Stability
Organism
pronase destroys activity
Histoplasma capsulatum
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
totally inhibits at very low concentrations
Histoplasma capsulatum
EGTA
totally inhibits at very low concentrations
Histoplasma capsulatum
o-phenanthroline
totally inhibits at very low concentrations
Histoplasma capsulatum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
L-cysteine
-
Histoplasma capsulatum
16.6
-
beta-mercaptoethanol
-
Histoplasma capsulatum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Histoplasma capsulatum
5829
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
stimulation, restores activity after inhibition with EDTA
Histoplasma capsulatum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10500
-
gel filtration, SDS-PAGE, the estimate of molecular weight may be inaccurate because it is based on use of the iodinated protein and the assumption that iodination does not affect molecular weight
Histoplasma capsulatum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-cysteine + O2
Histoplasma capsulatum
probable role in the mycelial to yeast phase transition
3-sulfino-L-alanine
-
Histoplasma capsulatum
?
Organism
Organism
UniProt
Commentary
Textmining
Histoplasma capsulatum
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
using filtration, centrifugation, column chromatography on DEAE-cellulose, Sephadex G-50 and cysteine-Sepharose
Histoplasma capsulatum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
no activity in mycelium
Histoplasma capsulatum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
6.31 atoms of oxygen/1000000 * min * mg protein
Histoplasma capsulatum
Storage Stability
Storage Stability
Organism
-70°C, crude enzyme, stable for up to 4 weeks
Histoplasma capsulatum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
beta-mercaptoethanol + O2
slight activity
439543
Histoplasma capsulatum
2-hydroxyethanesulfinate
-
439543
Histoplasma capsulatum
?
L-cysteine + O2
highly specific for L-cysteine
439543
Histoplasma capsulatum
3-sulfino-L-alanine
-
439543
Histoplasma capsulatum
?
L-cysteine + O2
probable role in the mycelial to yeast phase transition
439543
Histoplasma capsulatum
3-sulfino-L-alanine
-
439543
Histoplasma capsulatum
?
additional information
D-cysteine, cystine, taurine, cystamine, cysteinesulfinic acid, glutathione, cysteic acid, S-methylcysteine and pyruvic acid do not serve as substrates
439543
Histoplasma capsulatum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 10500, SDS-PAGE
Histoplasma capsulatum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
activity at 37°C 2-fold higher than at 25°C
Histoplasma capsulatum
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
37
activity at 37°C 2-fold higher than at 25°C
Histoplasma capsulatum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Histoplasma capsulatum
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
1 mol of enzyme contains about 0.1 mol of flavin
Histoplasma capsulatum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
NADH
stimulates
Histoplasma capsulatum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
1 mol of enzyme contains about 0.1 mol of flavin
Histoplasma capsulatum
General Stability (protein specific)
General Stability
Organism
pronase destroys activity
Histoplasma capsulatum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
totally inhibits at very low concentrations
Histoplasma capsulatum
EGTA
totally inhibits at very low concentrations
Histoplasma capsulatum
o-phenanthroline
totally inhibits at very low concentrations
Histoplasma capsulatum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
L-cysteine
-
Histoplasma capsulatum
16.6
-
beta-mercaptoethanol
-
Histoplasma capsulatum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Histoplasma capsulatum
5829
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
stimulation, restores activity after inhibition with EDTA
Histoplasma capsulatum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10500
-
gel filtration, SDS-PAGE, the estimate of molecular weight may be inaccurate because it is based on use of the iodinated protein and the assumption that iodination does not affect molecular weight
Histoplasma capsulatum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-cysteine + O2
Histoplasma capsulatum
probable role in the mycelial to yeast phase transition
3-sulfino-L-alanine
-
Histoplasma capsulatum
?
Purification (Commentary) (protein specific)
Commentary
Organism
using filtration, centrifugation, column chromatography on DEAE-cellulose, Sephadex G-50 and cysteine-Sepharose
Histoplasma capsulatum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
no activity in mycelium
Histoplasma capsulatum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
6.31 atoms of oxygen/1000000 * min * mg protein
Histoplasma capsulatum
Storage Stability (protein specific)
Storage Stability
Organism
-70°C, crude enzyme, stable for up to 4 weeks
Histoplasma capsulatum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
beta-mercaptoethanol + O2
slight activity
439543
Histoplasma capsulatum
2-hydroxyethanesulfinate
-
439543
Histoplasma capsulatum
?
L-cysteine + O2
highly specific for L-cysteine
439543
Histoplasma capsulatum
3-sulfino-L-alanine
-
439543
Histoplasma capsulatum
?
L-cysteine + O2
probable role in the mycelial to yeast phase transition
439543
Histoplasma capsulatum
3-sulfino-L-alanine
-
439543
Histoplasma capsulatum
?
additional information
D-cysteine, cystine, taurine, cystamine, cysteinesulfinic acid, glutathione, cysteic acid, S-methylcysteine and pyruvic acid do not serve as substrates
439543
Histoplasma capsulatum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 10500, SDS-PAGE
Histoplasma capsulatum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
activity at 37°C 2-fold higher than at 25°C
Histoplasma capsulatum
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
37
activity at 37°C 2-fold higher than at 25°C
Histoplasma capsulatum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Histoplasma capsulatum
Other publictions for EC 1.13.11.20
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)
742253
Pietra
On the dynamical behavior of ...
Rattus norvegicus
Chem. Biodivers.
14
e1700290
2017
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1
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1
-
3
-
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4
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2
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1
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1
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1
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4
-
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2
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-
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2
2
-
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-
742755
Faponle
Sulfoxide synthase versus cys ...
Rattus norvegicus
J. Am. Chem. Soc.
139
9259-9270
2017
-
-
-
-
-
-
-
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1
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1
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2
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1
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1
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1
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1
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2
2
-
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-
742264
Tchesnokov
An iron-oxygen intermediate f ...
Rattus norvegicus
Chem. Commun. (Camb.)
52
8814-8817
2016
-
-
1
-
1
-
-
1
-
1
-
1
-
1
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1
1
1
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3
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1
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1
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1
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1
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1
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1
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3
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1
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1
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743088
Driggers
Structure-based insights into ...
Rattus norvegicus
J. Mol. Biol.
428
3999-4012
2016
1
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1
3
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4
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1
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2
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1
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1
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2
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2
2
-
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-
741585
Arjune
Involvement of the Cys-Tyr co ...
Homo sapiens
Amino Acids
47
55-63
2015
-
-
1
-
1
-
3
3
-
1
-
1
-
3
-
1
-
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-
-
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1
-
1
1
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1
1
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1
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1
1
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1
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3
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3
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1
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1
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1
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1
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1
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1
1
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741704
Wenning
Substrate and cofactor range ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Appl. Environ. Microbiol.
82
910-921
2015
-
-
1
-
-
-
7
3
-
6
1
4
-
4
-
-
1
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-
-
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8
2
4
1
-
-
3
2
-
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2
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2
-
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-
8
-
3
-
8
1
4
-
-
-
2
-
-
-
-
8
2
2
-
-
3
2
-
-
2
-
2
2
-
3
3
742295
Sallmann
Structure and mechanism leadi ...
Homo sapiens
Chemistry
21
7470-7479
2015
-
-
-
-
-
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1
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1
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1
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1
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1
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1
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3
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2
2
-
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743757
Driggers
Structures of Arg- and Gln-ty ...
Bacillus subtilis 168, Bacillus subtilis
Protein Sci.
24
154-161
2015
-
-
1
1
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1
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2
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6
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1
1
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2
2
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741904
Davies
The Cys-Tyr cross-link of cys ...
Rattus norvegicus
Biochemistry
53
7961-7968
2014
-
-
1
1
1
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-
4
-
1
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1
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1
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1
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1
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1
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3
2
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1
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1
1
1
1
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4
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1
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1
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1
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1
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3
2
-
-
-
-
1
1
-
2
2
724391
Blaesi
Spectroscopic and computationa ...
Mus musculus
Biochemistry
52
6040-6051
2013
-
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1
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1
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1
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2
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1
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1
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1
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2
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1
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1
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2
2
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724396
Souness
Mechanistic implications of pe ...
Rattus norvegicus
Biochemistry
52
7606-7617
2013
-
-
1
1
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1
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1
1
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725651
Che
Metal vs. chalcogen competitio ...
Rattus norvegicus
J. Inorg. Biochem.
122
1-7
2013
-
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1
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2
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1
1
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725720
Driggers
Cysteine dioxygenase structure ...
Homo sapiens
J. Mol. Biol.
425
3121-3136
2013
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1
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1
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1
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1
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2
2
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725864
Kasperova
The possible role of dermatoph ...
Bacillus sp. (in: Bacteria), Candida albicans, Histoplasma capsulatum, Mammalia, Streptomyces sp., Trichophyton mentagrophytes, Trichophyton rubrum
Med. Mycol.
51
449-454
2013
-
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7
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10
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4
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7
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7
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7
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4
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7
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-
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15
15
-
-
-
724336
Tchesnokov
A strongly bound high-spin iro ...
Rattus norvegicus
Biochemistry
51
257-264
2012
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1
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1
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713084
Kasperova
Isolation of recombinant cyste ...
Trichophyton mentagrophytes, Trichophyton mentagrophytes TM-10
Mycoses
54
e456-462
2011
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1
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2
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5
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1
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1
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724297
Crawford
Single turnover of substrate-b ...
Mus musculus
Biochemistry
50
10241-10253
2011
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1
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1
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2
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1
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2
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1
1
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1
1
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1
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1
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Dominy
Identification and characteriz ...
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Stipanuk
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Parsons
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Rats fed a low protein diet su ...
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Bagley
The activities of rat hepatic ...
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McCann
Human cysteine dioxygenase typ ...
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Yamaguchi
Cysteine dioxygenase ...
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Kumar
Purification and characterizat ...
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1
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1
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1
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3
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2
3
1
1
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1
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1
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1
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Yamaguchi
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7
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16
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1
2
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1
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1
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2
1
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1
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Sakakibara
Purification and some properti ...
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Sakakibara
Two components of cysteine oxi ...
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