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

Reaction

AMP
+
sulfite
+
thioredoxin disulfide
=
5'-adenylyl sulfate
+
thioredoxin

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

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.10 adenylyl-sulfate reductase (thioredoxin)

Metals Ions

Metals Ions on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
activates
Fe-S center
-
in the native state, two clusters of the enzyme are in the [4Fe-4S]2+ oxidized state
Fe-S cluster
-
[4Fe-4S] cluster
Iron
-
4Fe-4S containing protein. Oxidation state of +2 for the 4Fe-4S cluster, with no disulfide bond in the holoenzyme
KNO3
-
activates
sulfate
-
activates
additional information
-
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