BRENDA - Enzyme Database
show all sequences of 1.8.4.8

Yeast PAPS reductase: properties and requirements of the purified enzyme

Schwenn, J.D.; Krone, F.A.; Husmann, K.; Arch. Microbiol. 150, 313-319 (1988)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
thioredoxin from Saccharomyces cerevisiae
-
Saccharomyces cerevisiae
0.0014
-
thioredoxin from Escherichia coli
-
Saccharomyces cerevisiae
0.019
-
5-Phosphoadenosine 3-phosphosulfate
with thioredoxin from Saccharomyces cerevisiae as cosubstrate
Saccharomyces cerevisiae
0.021
-
5-Phosphoadenosine 3-phosphosulfate
with thioredoxin from E. coli as cosubstrate
Saccharomyces cerevisiae
Organism
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Saccharomyces cerevisiae
Reaction
Reaction
Commentary
Organism
Reaction ID
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
from the kinetic data it is concluded that the enzyme follows an ordered mechanism with thioredoxin as the first substrate followed by 5-phosphoadenosine 3-phosphosulfate as the second
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
44.13
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
-
133775
Saccharomyces cerevisiae
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
133775
Saccharomyces cerevisiae
-
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
thioredoxin from Saccharomyces cerevisiae
-
Saccharomyces cerevisiae
0.0014
-
thioredoxin from Escherichia coli
-
Saccharomyces cerevisiae
0.019
-
5-Phosphoadenosine 3-phosphosulfate
with thioredoxin from Saccharomyces cerevisiae as cosubstrate
Saccharomyces cerevisiae
0.021
-
5-Phosphoadenosine 3-phosphosulfate
with thioredoxin from E. coli as cosubstrate
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
44.13
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
-
133775
Saccharomyces cerevisiae
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
133775
Saccharomyces cerevisiae
-
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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712502
Bhave
Spectroscopic studies on the [ ...
Mycobacterium tuberculosis
J. Biol. Chem.
286
1216-1226
2011
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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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685145
Chartron
3-Phosphoadenosine-5-phosphosu ...
Escherichia coli
Biochemistry
46
3942-3951
2007
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-
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
3
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2
1
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1
3
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8
1
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3
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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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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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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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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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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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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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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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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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1
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2
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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