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Literature summary for 7.2.2.9 extracted from
- Spectroscopic investigation of the reaction mechanism of CopB-B, the catalytic fragment from an archaeal thermophilic ATP-driven heavy metal transporter (2009), FEBS J., 276, 6172-6186.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | not necessary for nucleotide association but essential for the phosphatase activity | Saccharolobus solfataricus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q97UU7 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | study of the mechanism of ATP hydrolysis of a shortened variant of the heavy metal-translocating P-type ATPase CopB. Stoichiometric high-affinity binding of one nucleotide to the protein is demonstrated. The phosphate groups are not involved in nucleotide binding. A model of the hydrolytic mechanism is suggested | Saccharolobus solfataricus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CopV | - |
Saccharolobus solfataricus |
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