EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    1.8.4.9 | 3'-phosphoadenosine 5'-phosphosulfate + dithioerythritol |
- |
Physcomitrium patens |
? |
- |
? |
| 1.8.4.9 | adenosine 5'-phosphosulfate + glutathione |
PpAPR-B is much more active with adenosine 5'-phosphosulfate as a substrate than with 3'-phosphoadenosine 5'-phosphosulfate |
Physcomitrium patens |
? |
- |
? |
| 1.8.4.9 | adenylyl sulfate + DTT |
- |
Physcomitrium patens |
? |
- |
? |
| 1.8.4.9 | hydroxyethyldisulfide + glutathione |
catalyzed by the holoenzyme APR1p and the C-domain |
Arabidopsis thaliana |
? |
- |
? |
| 1.8.4.9 | more |
enzyme is involved in sulfate assimilation |
Arabidopsis thaliana |
? |
- |
? |
| 1.8.4.9 | more |
enzyme is involved in sulfate assimilation, influence of chilling stress on the intercellular distribution of assimilatory sulfate reduction and thiols, overview |
Zea mays |
? |
- |
? |
| 1.8.4.9 | more |
no activity with thioredoxin |
Physcomitrium patens |
? |
- |
? |
| 1.8.4.9 | more |
APR is the key enzyme of sulfate assimilation, extensive posttranscriptional regulation of plant APR, e.g. by salt stress, sulfate assimilation pathway is controlled by a complex network of multiple signals on different regulatory levels, overview |
Arabidopsis thaliana |
? |
- |
? |
| 1.8.4.9 | more |
the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes |
Physcomitrium patens |
? |
- |
? |
| 1.8.4.9 | more |
GSH is docked into the AtAPR1 redox domain active site by manual docking, superimposing the structures of glutaredoxin bound with GSH on that of the AtAPR1 redox domain. The structure of cGrx1 complexed with GSH (PDB code 4TR1) is used as a template. Interaction between GSH and the AtAPR1 redox domain is analyzed, binding structure analysis, overview |
Arabidopsis thaliana |
? |
- |
- |
