Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
(NH4)2SO4 | activates | Physcomitrium patens | |
KNO3 | activates | Physcomitrium patens | |
Mg2+ | activates | Physcomitrium patens | |
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 | Physcomitrium patens | |
sulfate | activates | Physcomitrium patens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl sulfate + thioredoxin | Physcomitrium patens | sulfate assimilation pathway in Physcomitrella patens, overview | AMP + sulfite + thioredoxin disulfide | - |
? | |
additional information | Physcomitrium patens | the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Physcomitrium patens | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin | the reaction catalyzed by APR can be divided into three steps. In the first step, APS binds to the protein, and a reductive transfer results in sulfite bound to the active-site cysteine in a stable reaction intermediate. In the second step, free sulfite is released by the action of free thioredoxin. In the third step, the thioredoxin is regenerated by reduction with thioredoxin reductase | Physcomitrium patens |
Storage Stability | Organism |
---|---|
-20°C, 1 day, PpAPR-B retains 30% of its activity | Physcomitrium patens |
4°C, PpAPR-B, completely stable for 5 days | Physcomitrium patens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl sulfate + thioredoxin | sulfate assimilation pathway in Physcomitrella patens, overview | Physcomitrium patens | AMP + sulfite + thioredoxin disulfide | - |
? | |
adenylyl sulfate + thioredoxin | dependent on thioredoxin, APS is the preferred substrate, substrate binding structure, modelling, overview | Physcomitrium patens | AMP + sulfite + thioredoxin disulfide | - |
? | |
additional information | 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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
APR | - |
Physcomitrium patens |
PpAPR-B | - |
Physcomitrium patens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Physcomitrium patens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
PpAPR-B activity in terms of APS reduction increases gradually and less markedly with increasing pH compared to PpAPR, EC 1.8.4.9 | Physcomitrium patens |
8 | - |
- |
Physcomitrium patens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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. No activity with glutathione or DTT | Physcomitrium patens | |
thioredoxin | - |
Physcomitrium patens |