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Literature summary for 7.2.2.8 extracted from
- Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus (2008), Arch. Biochem. Biophys., 471, 198-206.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Archaeoglobus fulgidus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O29777 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + Ag+[side 1] | Ag+-ATPase activity is measured as the difference between the activity in the medium with Ag+ and that measured in the same medium without Ag+ | Archaeoglobus fulgidus | ADP + phosphate + Ag+[side 2] | - |
? |  |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 66 | 85 | incubation of CopA in the absence of substrates at temperatures in the 6685°C range leads to an irreversible exponential decrease in enzyme activity suggesting a two-state process involving fully-active and inactive molecules. Although CopA inactivated much slower than mesophilic proteins, the activation energy is similar to that observed for mesophilic P-type ATPases. The inactivation process is found to be associated with the irreversible partial unfolding of the polypeptide chain. However, the inactive thermally denatured protein still conserves large hydrophobic regions and considerable secondary structure | Archaeoglobus fulgidus |
| 75 | - |
complete and irreversible inactivation after 70 min | Archaeoglobus fulgidus |
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