Cloned (Comment) | Organism |
---|---|
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified. Expressed protein generated from the ATP-sulfurylase domain alone is fully active in both the forward and the reverse assays. APS kinase-only recombinants exhibit no kinase activity | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + sulfate | - |
Mus musculus | diphosphate + adenylylsulfate | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme consists of a COOH-terminal ATP sulfurylase domain covalently linked through a nonhomologous intervening sequence to an NH2-terminal adenosine 5'-phosphosulfate kinase domain forming a bifunctional fused protein | Mus musculus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable | Mus musculus |
37 | - |
2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity | Mus musculus |