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Literature summary for 1.2.5.1 extracted from
- Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex (1985), J. Biol. Chem., 260, 10986-10990.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate + ubiquinone-8 + H2O | - |
Escherichia coli | acetate + CO2 + ubiquinol-8 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ubiquinone-dependent pyruvate oxidase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the cytochrome o complex functions as an efficient ubiquinol-8 oxidase in reconstituted proteoliposomes, and ubiquinone-8 serves as an electron carrier from the flavoprotein pyruvate oxidase to the cytochrome complex. Electron flow from the flavoprotein to oxygen in the reconstituted proteoliposomes generates a transmembrane potential of at least 120 mV, negative inside, which is sensitive to ionophore uncouplers and inhibitorso f the terminal oxidase. The minimal composition of this respiratory chain is a flavoprotein dehydrogenase, ubiquinone-8, and the cytochrome o complex | Escherichia coli |
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