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Literature summary extracted from
- Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus (2002), J. Biol. Chem., 277, 7201-7208.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.8 | additional information | dithiothreitol is necessary in the medium to maintain the metal in its Cu(I) redox state | Archaeoglobus fulgidus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.2.2.8 | expression in Escherichia coli | Archaeoglobus fulgidus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.8 | N-methylglucamine | - |
Archaeoglobus fulgidus |  |
| 7.2.2.8 | oligomycin | - |
Archaeoglobus fulgidus | |
| 7.2.2.8 | vanadate | - |
Archaeoglobus fulgidus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.8 | 0.25 | - |
ATP | pH 6.1, 75°C, ATPase activity | Archaeoglobus fulgidus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.8 | additional information | high salt concentration stimulate the ATPase, reaching a plateau at 400500 mM. This effect appears independent of the cation, since NaCl or KCl yields similar Ag-ATPase stimulation. Experiments using N-methylglucamine to increase ionic strength in the medium could not confirm this point. Although the amine at low concentration (under 10 mM) stimulats the ATPase as NaCl or KCl, it leads to a sharp inactivation at higher concentrations | Archaeoglobus fulgidus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.2.2.8 | Archaeoglobus fulgidus | O29777 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.2.2.8 | - |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.8 | ATP + H2O + Ag+[side 1] | the enzyme is activated by Ag+ and to a lesser extent by Cu+. Maximum Cu+-ATPase activity is 25% of that measured in the presence of Ag+. However, Cu+interacts with the enzyme with higher apparent affinity. The activation by Ag+ or Cu+is dependent on the presence of millimolar amounts of cysteine. In the presence of ATP, these metals drive the formation of an acid-stable phosphoenzyme with apparent affinities similar to those observed in the ATPase activity determinations. Comparable levels of phosphoenzyme are reached in the presence of both cations. The stimulation of phosphorylation by the cations suggests that CopA drives the outward movement of the metal | Archaeoglobus fulgidus | ADP + phosphate + Ag+[side 2] | - |
? | |
| 7.2.2.8 | ATP + H2O + Cu+[side 1] | the enzyme is activated by Ag+ and to a lesser extent by Cu+. Maximum Cu+-ATPase activity is 25% of that measured in the presence of Ag+.However, Cu+interacts with the enzyme with higher apparent affinity. The activation by Ag+ or Cu+is dependent on the presence of millimolar amounts of cysteine. In the presence of ATP, these metals drive the formation of an acid-stable phosphoenzyme with apparent affinities similar to those observed in the ATPase activity determinations. Comparable levels of phosphoenzyme are reached in the presence of both cations. The stimulation of phosphorylation by the cations suggests that CopA drives the outward movement of the metal | Archaeoglobus fulgidus | ADP + phosphate + Cu+[side 2] | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.2.8 | Ag+/Cu+-ATPase | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.8 | 75 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.8 | 60 | 80 | 60°C: about 55% of maximal activity, 80°C: about 75% of maximal activity | Archaeoglobus fulgidus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.8 | 6.1 | 6.5 | - |
Archaeoglobus fulgidus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.8 | 6 | 7 | pH 6.0: about 30% of maximal activity, pH 7.0: about 30% of maximal activity | Archaeoglobus fulgidus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.8 | 0.0047 | - |
oligomycin | pH 6.1, 75°C | Archaeoglobus fulgidus | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.8 | 0.024 | - |
pH 6.1, 75°C | Archaeoglobus fulgidus | vanadate | |
| 7.2.2.8 | 25 | - |
pH 6.1, 75°C | Archaeoglobus fulgidus | N-methylglucamine | |
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