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Literature summary extracted from
- Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase (2002), J. Biol. Chem., 277, 46987-46992.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.2.2.8 | C14A/C17A/C110A/C113A | increase in affinity for Cu(II) | Escherichia coli |
| 7.2.2.8 | C479A | mutation results in lost of resistance to copper | Escherichia coli |
| 7.2.2.8 | C481A | mutation results in lost of resistance to copper | Escherichia coli |
| 7.2.2.8 | C481H | mutation results in lost of resistance to copper | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.8 | Bathocuproine disulfonate | i.e. BCS, Cu(I) chelator, reduces enzyme activity | Escherichia coli |  |
| 7.2.2.8 | hydroxylamine | sensitive to | Escherichia coli | |
| 7.2.2.8 | KOH | sensitive to | Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.8 | 0.00045 | - |
Cu+ | apparent Km-value of C14A/C17A/C110A/C113A mutant protein, pH 6.8, 20°C | Escherichia coli | |
| 7.2.2.8 | 0.0015 | - |
Cu+ | apparent Km-value of wild-type protein, pH 6.8, 20°C | Escherichia coli | |
| 7.2.2.8 | 0.5 | - |
ATP | pH 6.8, 20°C | Escherichia coli | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.8 | Ag+ | stimulating | Escherichia coli | |
| 7.2.2.8 | Cu+ | stimulating | Escherichia coli | |
| 7.2.2.8 | additional information | divalent cations Cu(II), Zn(II), or Co(II) could not substitute Cu(I) or Ag(I) | Escherichia coli | |
| 7.2.2.8 | Sodium azide | inhibits ATP hydrolysis | Escherichia coli | |
| 7.2.2.8 | vanadate | inhibitor | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.8 | ATP + H2O + Cu+ | Escherichia coli | - |
ADP + phosphate + Cu+ | - |
? | |
| 7.2.2.8 | ATP + H2O + Cu+[side 1] | Escherichia coli | CopA forms a phosphorylated intermediate | ADP + phosphate + Cu+[side 2] | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.2.2.8 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.2.2.8 | CopA purified from dodecylmaltoside-solubilized membranes by metal chelate affinity chromatography, presence of a small amount of copper during solubilization and purification found to result in a more active and stable CopA | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.8 | ATP + H2O + Cu+ | - |
Escherichia coli | ADP + phosphate + Cu+ | - |
? | |
| 7.2.2.8 | ATP + H2O + Cu+[side 1] | CopA forms a phosphorylated intermediate | Escherichia coli | ADP + phosphate + Cu+[side 2] | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.2.8 | CopA | - |
Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.2.2.8 | physiological function | Escherichia coli CopA is a copper ion-translocating P-type ATPase that confers copper resistance | Escherichia coli |
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