1.8.4.8 3'-adenylyl-sulfate + thioredoxin - Bacillus subtilis adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite - ? 374986 1.8.4.8 3'-phosphoadenylyl sulfate + glutaredoxin 1 - Bacillus subtilis adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide - r 451785 1.8.4.8 3'-phosphoadenylyl sulfate + glutaredoxin 1 - Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide - r 451785 1.8.4.8 3'-phosphoadenylyl sulfate + glutaredoxin Grx poplar glutaredoxin, 33% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx disulfide - ? 440736 1.8.4.8 3'-phosphoadenylyl sulfate + glutaredoxin Grx1 Escherichia coli glutaredoxin, 70% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx1 disulfide - ? 440735 1.8.4.8 3'-phosphoadenylyl sulfate + glutaredoxin mutant 1C14S - Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin mutant 1C14S disulfide - r 451786 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin thioredoxin from Escherichia coli Saccharomyces cerevisiae adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide - r 451784 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin thioredoxin from Saccharomyces cerevisiae Saccharomyces cerevisiae adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide - r 451784 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin 1 - Bacillus subtilis adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide - r 451787 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin 1 - Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide - r 451787 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin 2 - Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin 2 disulfide - r 451788 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin hTrx1 human thioredoxin, 59% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin hTrx1 disulfide - ? 440737 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin Trx1 Escherichia coli thioredoxin Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx1 disulfide - ? 440738 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin Trx2 Escherichia coli thioredoxin, 38% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx2 disulfide - ? 440739 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin TrxH1 Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH1 disulfide - ? 440740 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin TrxH2 Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide - ? 440741 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin TrxH3 Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide - ? 440742 1.8.4.8 3'-phosphoadenylyl sulfate + thioredoxin TrxH4 Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide - ? 440743 1.8.4.8 3'-phosphoadenylyl-sulfate + glutaredoxin - Bacillus subtilis adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite - ? 374985 1.8.4.8 3'-phosphoadenylyl-sulfate + glutaredoxin - Escherichia coli adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite - ? 374985 1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin - Bacillus subtilis adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite - ? 374994 1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin - Escherichia coli adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite - ? 374994 1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin enzyme catalyzes the first reductive step in sulfate assimilation Escherichia coli adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite - ? 374994 1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin thioredoxin m from spinach Escherichia coli adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite - ? 374994 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin - Escherichia coli adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite - ? 92823 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin - Saccharomyces cerevisiae adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite - ? 92823 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin - Synechococcus sp. adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite - ? 92823 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin - Synechococcus sp. PCC 7942 adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite - ? 92823 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin enzyme is involved in sulfur metabolism Escherichia coli ? - ? 369715 1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth Escherichia coli ? - ? 369715 1.8.4.8 adenosine 5'-phosphosulfate + thioredoxin - Mycobacterium tuberculosis AMP + sulfite + oxidized thioredoxin - ? 414245 1.8.4.8 adenosine 5'-phosphosulfate + thioredoxin I - Pseudomonas aeruginosa AMP + sulfite + oxidized thioredoxin I - ? 414244 1.8.4.8 additional information enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview Escherichia coli ? - ? 89 1.8.4.8 additional information enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview Escherichia coli ? - ? 89 1.8.4.8 additional information thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction Escherichia coli ? - ? 89 1.8.4.8 additional information cofactor specificity Escherichia coli ? - ? 89 1.8.4.8 additional information 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 Pseudomonas aeruginosa ? - ? 89 1.8.4.8 additional information 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 Escherichia coli ? - ? 89