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
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Cofactor
Cofactor on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)
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thioredoxin
5fold lower activity with dithiothreithol, 70fold lower activity with E. coli Grx1 or dithionite, 580fold lower activity with lipoic acid, no activity with ferredoxin
thioredoxin
activity drops approx. 5fold in the absence of thioredoxin, glutathione can not replace thioredoxin
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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
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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. No activity with glutathione or DTT
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