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Literature summary 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.
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.2.5.1 | Escherichia coli | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.2.5.1 | 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]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.2.5.1 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.2.5.1 | pyruvate + ferricyanide + H2O | - |
Escherichia coli | acetate + CO2 + ferrocyanide | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.2.5.1 | pyruvate oxidase | - |
Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.2.5.1 | 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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Release 2023.1 (January 2023)
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