1.8.4.10: adenylyl-sulfate reductase (thioredoxin)
This is an abbreviated version!
For detailed information about adenylyl-sulfate reductase (thioredoxin), go to the full flat file.
Word Map on EC 1.8.4.10
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1.8.4.10
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aeruginosa
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sulfur
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thioredoxins
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reductases
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gamma-glutamylcysteine
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physcomitrella
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moss
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thiosulfate
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assimilatory
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patens
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two-electron
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analysis
- 1.8.4.10
- aeruginosa
- sulfur
- thioredoxins
- reductases
- gamma-glutamylcysteine
-
physcomitrella
-
moss
- thiosulfate
-
assimilatory
- patens
-
two-electron
- analysis
Reaction
Synonyms
5'-adenylylsulfate reductase, adenosine-5'-phosphosulfate reductase, adenylylsulfate reductase, APR, APR-B, APS reductase, PaAPR, PpAPR-B, thioredoxin dependent 5'-adenylylsulfate reductase, thioredoxin-dependent APS reductase
ECTree
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Metals Ions
Metals Ions on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)
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Fe-S center
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in the native state, two clusters of the enzyme are in the [4Fe-4S]2+ oxidized state
Iron
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4Fe-4S containing protein. Oxidation state of +2 for the 4Fe-4S cluster, with no disulfide bond in the holoenzyme
Mg2+
additional information
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PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein