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