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Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin) for references in articles please use BRENDA:EC1.8.4.8
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EC Tree
IUBMB Comments Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
The enzyme appears in viruses and cellular organisms
Synonyms
3'-Phosphoadenosine 5'-phosphosulfate reductase, 3'-Phosphoadenylylsulfate reductase, 4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase, 5'-adenylylsulfate reductase, Adenosine 3'-phosphate 5'-phosphosulfate reductase, adenosine 5'-phosphosulfate reductase, Adenylyl phosphosulfate reductase, APR, APS reductase, CysH1,
more
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3'-Phosphoadenosine 5'-phosphosulfate reductase
3'-Phosphoadenylylsulfate reductase
4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase
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5'-adenylylsulfate reductase
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Adenosine 3'-phosphate 5'-phosphosulfate reductase
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adenosine 5'-phosphosulfate reductase
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Adenylyl phosphosulfate reductase
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PAPS reductase, thioredoxin dependent
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PAPS reductase, thioredoxin-dependent
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PAPS sulfotransferase
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Phospho-adenylylsulfate (PAPS) reductase
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Phospho-adenylylsulfate reductase
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Reductase, 3'-phosphoadenosine 5'-phosphosulfate
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Thioredoxin: 3'-phospho-adenylylsulfate reductase
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Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
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3'-Phosphoadenosine 5'-phosphosulfate reductase
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3'-Phosphoadenosine 5'-phosphosulfate reductase
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3'-Phosphoadenosine 5'-phosphosulfate reductase
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3'-Phosphoadenylylsulfate reductase
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3'-Phosphoadenylylsulfate reductase
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APR
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APS reductase
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PAPS reductase
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
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
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
special ping-pong mechanism with 5-phosphoadenosine 3-phosphosulfate reacting with the reduced enzyme isomer in a Theorell-Chance mechanism
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism, Cys239 is the active site residue
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adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
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3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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?
3'-phosphoadenylyl sulfate + glutaredoxin Grx
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx disulfide
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poplar glutaredoxin, 33% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + glutaredoxin Grx1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx1 disulfide
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Escherichia coli glutaredoxin, 70% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin hTrx1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin hTrx1 disulfide
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human thioredoxin, 59% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin Trx1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx1 disulfide
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Escherichia coli thioredoxin
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?
3'-phosphoadenylyl sulfate + thioredoxin Trx2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx2 disulfide
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Escherichia coli thioredoxin, 38% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin TrxH1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH1 disulfide
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Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin TrxH2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide
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Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin TrxH3
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide
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Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl sulfate + thioredoxin TrxH4
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide
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Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1
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?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + oxidized thioredoxin
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?
adenosine 5'-phosphosulfate + thioredoxin I
AMP + sulfite + oxidized thioredoxin I
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?
additional information
?
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3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
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?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
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?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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enzyme catalyzes the first reductive step in sulfate assimilation
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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thioredoxin m from spinach
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
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enzyme is involved in sulfur metabolism
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
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essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
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additional information
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enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview
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additional information
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enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
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additional information
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thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
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additional information
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cofactor specificity
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additional information
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the redox potential does not determine specificity nor efficiency of the redoxins as reductant. The efficiency of PAPS reductase with various redoxins correlates strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces
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additional information
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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
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3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
additional information
?
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3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
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?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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enzyme catalyzes the first reductive step in sulfate assimilation
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
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enzyme is involved in sulfur metabolism
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
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essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
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additional information
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enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview
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additional information
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enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
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additional information
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thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
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4Fe-4S-center
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the enzyme harbors a [4Fe-4S]2+ cluster
glutaredoxin
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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
glutaredoxin
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glutaredoxin 1 variant
thioredoxin
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thioredoxin
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2 variants Trx1 and Trx2, equally active
thioredoxin
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thioredoxin 1 variant
thioredoxin
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dependent on
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Fe
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iron-sulfur protein, each mole of protein contains 3.3 mol of Fe
Iron
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the enzyme contains a [4Fe-4S] cluster per subunit, absolutely required for activity, constitution is altered in presence of oxygen, activity is restored after decomposition and reassembly
additional information
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enzyme contains no iron
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adenosine 3',5'-bisphosphate
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competitive with respect to 5-phosphoadenosine 3-phosphosulfate
glutathione
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0.002 to 0.6 mM
N-(Iodoacetyl-aminoethyl)-5-N'-naphthylamin-1-sulfonic acid
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oxidized glutathione
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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
p-chloromercuribenzoate
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glutaredoxin
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required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
additional information
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The activity of 3'-phosphoadenosine 5'-phosphosulfate reductase is increased by sulfur starvation
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0.0287 - 0.1054
3'-phosphoadenylyl sulfate
0.0064 - 0.0225
3'-phosphoadenylyl-sulfate
0.01 - 0.021
5-Phosphoadenosine 3-phosphosulfate
0.0149 - 0.0606
glutaredoxin 1
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0.0637
glutaredoxin Grx
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pH 8.0, temperature not specified in the publication
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0.0149
glutaredoxin Grx1
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pH 8.0, temperature not specified in the publication
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0.0072
glutaredoxin mutant 1C14S
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pH 8.0
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0.023
reduced thioredoxin
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0.0137 - 0.0675
thioredoxin 1
0.0342
thioredoxin 2
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pH 8.0
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0.0014
thioredoxin from Escherichia coli
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0.0006
thioredoxin from Saccharomyces cerevisiae
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0.0681
thioredoxin hTrx1
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pH 8.0, temperature not specified in the publication
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0.01
thioredoxin I
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wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
0.0137
thioredoxin Trx1
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pH 8.0, temperature not specified in the publication
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0.0342
thioredoxin Trx2
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pH 8.0, temperature not specified in the publication
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0.059
thioredoxin TrxH1
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pH 8.0, temperature not specified in the publication
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0.0431
thioredoxin TrxH2
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pH 8.0, temperature not specified in the publication
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0.0178
thioredoxin TrxH3
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pH 8.0, temperature not specified in the publication
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0.0261
thioredoxin TrxH4
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pH 8.0, temperature not specified in the publication
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additional information
additional information
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kinetics
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0.0287
3'-phosphoadenylyl sulfate
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recombinant enzyme, pH 8.0, with thioredoxin 1
0.1054
3'-phosphoadenylyl sulfate
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recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0064
3'-phosphoadenylyl-sulfate
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recombinant enzyme, pH 8.0, with thioredoxin 1
0.0107
3'-phosphoadenylyl-sulfate
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recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0225
3'-phosphoadenylyl-sulfate
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with cofactors Trx1, Trx2, or Grx1, pH 8.0
0.01
5-Phosphoadenosine 3-phosphosulfate
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0.019
5-Phosphoadenosine 3-phosphosulfate
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with thioredoxin from Saccharomyces cerevisiae as cosubstrate
0.021
5-Phosphoadenosine 3-phosphosulfate
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with thioredoxin from E. coli as cosubstrate
0.0149
glutaredoxin 1
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pH 8.0
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0.0225
glutaredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
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0.0606
glutaredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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0.0137
thioredoxin 1
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pH 8.0
0.0543
thioredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.0675
thioredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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0.149 - 0.335
3'-phosphoadenylyl sulfate
0.172 - 3.5
3'-phosphoadenylyl-sulfate
0.146 - 0.421
glutaredoxin 1
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0.174 - 0.219
thioredoxin 1
0.149
3'-phosphoadenylyl sulfate
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recombinant enzyme, pH 8.0, with thioredoxin 1
0.335
3'-phosphoadenylyl sulfate
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recombinant enzyme, pH 8.0, with glutaredoxin 1
0.172
3'-phosphoadenylyl-sulfate
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recombinant enzyme, pH 8.0, with thioredoxin 1
0.382
3'-phosphoadenylyl-sulfate
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recombinant enzyme, pH 8.0, with glutaredoxin 1
3.5
3'-phosphoadenylyl-sulfate
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pH 9.2-9.3, 35°C
0.146
glutaredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
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0.421
glutaredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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0.174
thioredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.219
thioredoxin 1
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recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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0.04 - 2500
adenosine 5'-phosphosulfate
0.04
adenosine 5'-phosphosulfate
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mutant enzyme K144A, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
2500
adenosine 5'-phosphosulfate
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wild type enzyme, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
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additional information
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additional information
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cofactor specificity
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8
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assay at
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gene cysH, bispecific enzyme
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
PCC7942
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brenda
PCC7942
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brenda
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brenda
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Uniprot
brenda
K12
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brenda
recombinant enzyme
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brenda
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Escherichia coli (strain K12)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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22635
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x * 22635, calculation from nucleotide sequence
27000
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2 * 27000, SDS-PAGE
27927
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2 * 27927, calculation from nucleotide sequence
44000
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reduction of the enzyme by dithiothreitol results in a shift of the apparent MW to 62000 without formation of an enzyme-thioredoxin complex, HPLC gel filtration
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?
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x * 30634.4, recombinant enzyme, mass spectrometry
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x * 22635, calculation from nucleotide sequence
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x * 22635, calculation from nucleotide sequence
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dimer
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2 * 27000, SDS-PAGE
dimer
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homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
dimer
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2 * 27927, calculation from nucleotide sequence
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crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold
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crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate reductase in complex with Escherichia coli thioredoxin 1 determined to 3.0 A resolution, crystals are grown by vapor diffusion in sitting drops
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C239S
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mutant enzymes Cys239Ser and Tyr209Phe are inactive
Q160L
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mutant enzyme Gln160Leu is as active as the wild-type enzyme
Y209F
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mutant enzymes Cys239Ser and Tyr209Phe are inactive
K144A |
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the mutation causes a 63000fold increase of kcat/KM and decreases the value of kmax by 270fold. Relative to the wild type enzyme, the affinity of adenosine 5’-phosphosulfate for K144A is decreased by 400fold
additional information
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a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
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activity is lost upon exposure to air or upon dilution
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activity is lost upon exposure to air
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659441
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HiTrap chelating column chromatography and Superdex 200 gel filtration
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recombinant enzyme from strain BL21(DE3)
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recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
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recombinant His10-tagged enzyme from strain BL21(DE3) by chelate affinity chromatography
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DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in strain BL21(DE3) as His-tagged protein
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expressed in Escherichia coli BL21(DE3) cells
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expression in strain BL21(DE3) as His10-tagged protein
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gene cysH, expression in Escherichia coli strain BL21(DE3)
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overexpression in strain BL21(DE3)
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medicine
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in Mycobacterium tuberculosis, APR is a validated target against the latent phase of infection
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Schwenn, J.D.; Krone, F.A.; Husmann, K.
Yeast PAPS reductase: properties and requirements of the purified enzyme
Arch. Microbiol.
150
313-319
1988
Saccharomyces cerevisiae
brenda
Savage, H.; Montoya, G.; Svensson, C.; Schwenn, J.D.; Sinning, I.
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases
Structure
5
895-906
1997
Escherichia coli
brenda
Montoya, G.; Svensson, C.; Savage, H.; Schwenn, J.D.; Sinning, I.
Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli
Acta Crystallogr. Sect. D
54
281-283
1998
Escherichia coli
brenda
Berendt, U.; Haverkamp, T.; Prior, A.; Schwenn, J.D.
Reaction mechanism of thioredoxin:3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis
Eur. J. Biochem.
233
347-356
1995
Escherichia coli
brenda
Niehaus, A.; Gisselmann, G.; Schwenn, J.D.
Primary structure of Synechococcus PCC 7942 PAPS reductase gene
Plant Mol. Biol.
20
1179-1183
1992
Synechococcus sp., Synechococcus sp. PCC 7942
brenda
Krone, A.; Westphal, G.; Schwenn, J.D.
Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli
Mol. Gen. Genet.
225
314-319
1991
Escherichia coli
brenda
Kopriva, S.; Buchert, T.; Fritz, G.; Suter, M.; Benda, R.; Schunemann, V.; Koprivova, A.; Schurmann, P.; Trautwein, A.X.; Kroneck, P.M.H.; Brunold, C.
The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation
J. Biol. Chem.
277
21786-21791
2002
Escherichia coli
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