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3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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3'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
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 + glutaredoxin mutant 1C14S
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin mutant 1C14S disulfide
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r
3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
3'-phosphoadenylyl sulfate + thioredoxin 2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 2 disulfide
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r
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
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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 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
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r
3'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
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3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
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thioredoxin from Escherichia coli
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3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
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thioredoxin from Saccharomyces cerevisiae
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3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
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3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
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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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