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Literature summary for 1.2.5.1 extracted from
- Rate constants in two dimensions of electron transfer between pyruvate oxidase, a membrane enzyme, and ubiquinone (coenzyme Q8), its water-insoluble electron carrier (2001), Biochemistry, 40, 1248-1256.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| reconstitution of enzyme with a supported lipidic structure. The activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 270 | - |
270 micromol of ferricyanide min-1 mg-1 of flavoprotein subunit, 25°C, pH not specified in the publication | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate + ferricyanide + H2O | - |
Escherichia coli | acetate + CO2 + ferrocyanide | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pyruvate oxidase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes | Escherichia coli |
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