BRENDA - Enzyme Database
show all sequences of 1.8.4.8

Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase

Chung, J.S.; Noguera-Mazon, V.; Lancelin, J.M.; Kim, S.K.; Hirasawa, M.; Hologne, M.; Leustek, T.; Knaff, D.B.; J. Biol. Chem. 284, 31181-31189 (2009)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
thioredoxin I
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
Pseudomonas aeruginosa
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
adenosine 5'-phosphosulfate + thioredoxin I
-
698950
Pseudomonas aeruginosa
AMP + sulfite + oxidized thioredoxin I
-
-
-
?
additional information
thioredoxin I mutant W31A shows no detectable activity, whereas W31F, K36E, and D61N are able to serve as electron donors for the APR-catalyzed reaction but with lower turnover numbers than that exhibited by the wild type thioredoxin I. The Km for thioredoxin mutant R73E is increased by 7.7fold compared with wild type thioredoxin I
698950
Pseudomonas aeruginosa
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
5'-adenylylsulfate reductase
-
Pseudomonas aeruginosa
APR
-
Pseudomonas aeruginosa
APS reductase
-
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
thioredoxin
dependent on
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
thioredoxin
dependent on
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
thioredoxin I
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
Pseudomonas aeruginosa
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
adenosine 5'-phosphosulfate + thioredoxin I
-
698950
Pseudomonas aeruginosa
AMP + sulfite + oxidized thioredoxin I
-
-
-
?
additional information
thioredoxin I mutant W31A shows no detectable activity, whereas W31F, K36E, and D61N are able to serve as electron donors for the APR-catalyzed reaction but with lower turnover numbers than that exhibited by the wild type thioredoxin I. The Km for thioredoxin mutant R73E is increased by 7.7fold compared with wild type thioredoxin I
698950
Pseudomonas aeruginosa
?
-
-
-
-
Other publictions for EC 1.8.4.8
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)
742273
Berndt
-
The specificity of thioredoxi ...
Escherichia coli
Chem. Sci.
6
7049-7058
2015
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9
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1
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10
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1
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10
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712502
Bhave
Spectroscopic studies on the [ ...
Mycobacterium tuberculosis
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286
1216-1226
2011
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1
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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2
2
698950
Chung
Interaction domain on thioredo ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
31181-31189
2009
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1
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1
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4
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685145
Chartron
3-Phosphoadenosine-5-phosphosu ...
Escherichia coli
Biochemistry
46
3942-3951
2007
-
-
1
1
-
-
-
-
-
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2
-
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1
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670348
Mansouri-Bauly
Sulfur uptake in the ectomycor ...
Laccaria bicolor, Laccaria bicolor S238N
Mycorrhiza
16
421-427
2006
1
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1
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9
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659441
Berndt
Characterization and reconstit ...
Bacillus subtilis
J. Biol. Chem.
279
7850-7855
2004
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-
1
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1
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8
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1
1
3
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2
1
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1
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3
1
3
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8
1
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2
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2
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1
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8
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1
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3
1
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8
1
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659214
Lillig
Redox regulation of 3'-phospho ...
Escherichia coli
J. Biol. Chem.
278
22325-22330
2003
1
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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
1
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1
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393953
Kopriva
The presence of an iron-sulfur ...
Escherichia coli
J. Biol. Chem.
277
21786-21791
2002
-
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1
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1
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2
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12
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1
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3
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2
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659140
Lillig
New thioredoxins and glutaredo ...
Escherichia coli
J. Biol. Chem.
274
7695-7698
1999
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1
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6
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2
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4
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1
1
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1
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5
1
2
1
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1
1
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2
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1
2
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6
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2
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1
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5
1
1
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1
1
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133777
Montoya
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
54
281-283
1998
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1
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2
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133776
Savage
Crystal structure of phosphoad ...
Escherichia coli
Structure
5
895-906
1997
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133778
Berendt
Reaction mechanism of thioredo ...
Escherichia coli
Eur. J. Biochem.
233
347-356
1995
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3
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4
2
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2
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1
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1
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1
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133779
Niehaus
Primary structure of Synechoco ...
Synechococcus sp., Synechococcus sp. PCC 7942
Plant Mol. Biol.
20
1179-1183
1992
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25
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1
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1
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133780
Krone
Characterisation of the gene c ...
Escherichia coli
Mol. Gen. Genet.
225
314-319
1991
-
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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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133775
Schwenn
Yeast PAPS reductase: properti ...
Saccharomyces cerevisiae
Arch. Microbiol.
150
313-319
1988
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4
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3
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1
1
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1
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1
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