BRENDA - Enzyme Database
show all sequences of 1.8.4.8

New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase

Lillig, C.H.; Prior, A.; Schwenn, J.D.; Aslund, F.; Ritz, D.; Vlamis-Gardikas, A.; Holmgren, A.; J. Biol. Chem. 274, 7695-7698 (1999)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in strain BL21(DE3) as His10-tagged protein
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Escherichia coli
0.0072
-
glutaredoxin mutant 1C14S
pH 8.0
Escherichia coli
0.0137
-
thioredoxin 1
pH 8.0
Escherichia coli
0.0149
-
glutaredoxin 1
pH 8.0
Escherichia coli
0.0225
-
3'-phosphoadenylyl-sulfate
with cofactors Trx1, Trx2, or Grx1, pH 8.0
Escherichia coli
0.0342
-
thioredoxin 2
pH 8.0
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3'-phosphoadenylyl-sulfate + thioredoxin
Escherichia coli
enzyme catalyzes the first reductive step in sulfate assimilation
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
?
additional information
Escherichia coli
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His10-tagged enzyme from strain BL21(DE3) by chelate affinity chromatography
Escherichia coli
Reaction
Reaction
Commentary
Organism
Reaction ID
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
cofactor specificity
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3'-phosphoadenylyl-sulfate + glutaredoxin
-
659140
Escherichia coli
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
-
659140
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
enzyme catalyzes the first reductive step in sulfate assimilation
659140
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
additional information
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
659140
Escherichia coli
?
-
-
-
-
additional information
cofactor specificity
659140
Escherichia coli
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 30634.4, recombinant enzyme, mass spectrometry
Escherichia coli
Synonyms
Synonyms
Commentary
Organism
3'-Phosphoadenylylsulfate reductase
-
Escherichia coli
PAPS reductase
-
Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.5
-
3'-phosphoadenylyl-sulfate
pH 9.2-9.3, 35°C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.2
9.3
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
glutaredoxin
in vitro, variant Grx1 is active similar to the thioredoxins, while Grx2 and Grx3 are not active, and a mutant form Grx1C14S is a poor cofactor
Escherichia coli
thioredoxin
2 variants Trx1 and Trx2, equally active
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in strain BL21(DE3) as His10-tagged protein
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
glutaredoxin
in vitro, variant Grx1 is active similar to the thioredoxins, while Grx2 and Grx3 are not active, and a mutant form Grx1C14S is a poor cofactor
Escherichia coli
thioredoxin
2 variants Trx1 and Trx2, equally active
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Escherichia coli
0.0072
-
glutaredoxin mutant 1C14S
pH 8.0
Escherichia coli
0.0137
-
thioredoxin 1
pH 8.0
Escherichia coli
0.0149
-
glutaredoxin 1
pH 8.0
Escherichia coli
0.0225
-
3'-phosphoadenylyl-sulfate
with cofactors Trx1, Trx2, or Grx1, pH 8.0
Escherichia coli
0.0342
-
thioredoxin 2
pH 8.0
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3'-phosphoadenylyl-sulfate + thioredoxin
Escherichia coli
enzyme catalyzes the first reductive step in sulfate assimilation
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
?
additional information
Escherichia coli
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His10-tagged enzyme from strain BL21(DE3) by chelate affinity chromatography
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
cofactor specificity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3'-phosphoadenylyl-sulfate + glutaredoxin
-
659140
Escherichia coli
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
-
659140
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
enzyme catalyzes the first reductive step in sulfate assimilation
659140
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
additional information
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
659140
Escherichia coli
?
-
-
-
-
additional information
cofactor specificity
659140
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 30634.4, recombinant enzyme, mass spectrometry
Escherichia coli
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.5
-
3'-phosphoadenylyl-sulfate
pH 9.2-9.3, 35°C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.2
9.3
-
Escherichia coli
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
-
-
-
-
-
-
-
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
10
-
1
-
-
-
-
-
-
-
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-
-
-
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-
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9
-
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-
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-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712502
Bhave
Spectroscopic studies on the [ ...
Mycobacterium tuberculosis
J. Biol. Chem.
286
1216-1226
2011
-
1
1
-
1
-
-
-
-
1
-
-
-
3
-
-
1
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
1
-
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-
-
1
1
1
-
1
-
-
-
-
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1
-
-
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-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
698950
Chung
Interaction domain on thioredo ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
31181-31189
2009
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
3
-
-
-
-
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-
-
1
-
-
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-
1
1
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1
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1
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-
-
-
2
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
685145
Chartron
3-Phosphoadenosine-5-phosphosu ...
Escherichia coli
Biochemistry
46
3942-3951
2007
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
1
-
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1
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1
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1
-
-
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-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
670348
Mansouri-Bauly
Sulfur uptake in the ectomycor ...
Laccaria bicolor, Laccaria bicolor S238N
Mycorrhiza
16
421-427
2006
1
-
-
-
-
-
1
-
-
-
-
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-
9
-
-
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-
-
-
-
-
-
659441
Berndt
Characterization and reconstit ...
Bacillus subtilis
J. Biol. Chem.
279
7850-7855
2004
-
-
1
-
-
1
-
8
-
1
1
3
-
2
1
-
-
-
-
-
1
-
3
1
3
-
-
-
8
1
-
-
2
-
-
-
-
-
1
2
-
-
1
-
-
-
8
-
1
1
3
-
1
-
-
-
-
1
-
3
1
-
-
-
8
1
-
-
-
-
-
-
-
-
-
659214
Lillig
Redox regulation of 3'-phospho ...
Escherichia coli
J. Biol. Chem.
278
22325-22330
2003
1
-
1
-
1
-
1
-
-
-
-
3
-
2
-
-
1
1
-
-
-
-
3
-
2
1
-
-
-
1
-
-
2
-
-
-
1
-
1
2
-
1
-
-
1
-
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-
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3
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
393953
Kopriva
The presence of an iron-sulfur ...
Escherichia coli
J. Biol. Chem.
277
21786-21791
2002
-
-
1
-
-
-
-
-
-
1
-
2
-
12
-
-
1
-
-
-
-
-
3
-
2
-
-
-
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-
-
1
-
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1
1
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1
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2
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1
-
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-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659140
Lillig
New thioredoxins and glutaredo ...
Escherichia coli
J. Biol. Chem.
274
7695-7698
1999
-
-
1
-
-
-
-
6
-
-
-
2
-
4
-
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1
1
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-
1
-
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
-
-
1
-
5
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
133777
Montoya
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
54
281-283
1998
-
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-
1
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1
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2
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2
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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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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
1
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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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4
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1
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1
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