BRENDA - Enzyme Database
show all sequences of 1.8.4.8

Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins

Lillig, C.H.; Potamitou, A.; Schwenn, J.D.; Vlamis-Gardikas, A.; Holmgren, A.; J. Biol. Chem. 278, 22325-22330 (2003)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
glutaredoxin
required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
Escherichia coli
Cloned(Commentary)
Cloned (Commentary)
Organism
overexpression in strain BL21(DE3)
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
additional information
a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
oxidized glutathione
reversible inhibition, forms mixed disulfides with the enzymes active site residue Cys239, inactivation kinetics, inhibition is reversible by glutaredoxin, not by DTT, glutaredoxin together with glutathione exhibits regulatory function in vivo
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 + glutaredoxin
Escherichia coli
-
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
Escherichia coli
-
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
?
additional information
Escherichia coli
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme from strain BL21(DE3)
Escherichia coli
Reaction
Reaction
Commentary
Organism
Reaction ID
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism, Cys239 is the active site residue
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
-
659214
Escherichia coli
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
-
659214
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
additional information
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
659214
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
30
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
glutaredoxin
-
Escherichia coli
thioredoxin
-
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
glutaredoxin
required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in strain BL21(DE3)
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
glutaredoxin
-
Escherichia coli
thioredoxin
-
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
oxidized glutathione
reversible inhibition, forms mixed disulfides with the enzymes active site residue Cys239, inactivation kinetics, inhibition is reversible by glutaredoxin, not by DTT, glutaredoxin together with glutathione exhibits regulatory function in vivo
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 + glutaredoxin
Escherichia coli
-
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
Escherichia coli
-
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
?
additional information
Escherichia coli
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from strain BL21(DE3)
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
-
659214
Escherichia coli
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
-
659214
Escherichia coli
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
?
additional information
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
659214
Escherichia coli
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Other publictions for EC
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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9
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10
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712502
Bhave
Spectroscopic studies on the [ ...
Mycobacterium tuberculosis
J. Biol. Chem.
286
1216-1226
2011
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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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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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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
-
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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1
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8
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1
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1
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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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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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1
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1
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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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4
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6
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2
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1
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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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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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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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133780
Krone
Characterisation of the gene c ...
Escherichia coli
Mol. Gen. Genet.
225
314-319
1991
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133775
Schwenn
Yeast PAPS reductase: properti ...
Saccharomyces cerevisiae
Arch. Microbiol.
150
313-319
1988
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