Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli GR19N | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-lactate + ferricyanide | - |
Escherichia coli | pyruvate + ferrocyanide | - |
? | |
D-lactate + ferricyanide | - |
Escherichia coli GR19N | pyruvate + ferrocyanide | - |
? | |
D-lactate + ubiquinone 1 | - |
Escherichia coli | pyruvate + reduced ubiquinone 1 | - |
? | |
D-lactate + ubiquinone 1 | - |
Escherichia coli GR19N | pyruvate + reduced ubiquinone 1 | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | D-lactate/ubiquinone 1 or D-lactate/ferricyanide oxidoreductase activity does not generate a membranepotential, suggesting that electron flow from D-lactate dehydrogenase to ubiquinone is not electrogenic. Proteoliposomes reconstituted with purified D-lactate dehydrogenase, ubiquinone 8, and purified cytochrome o catalyze D-lactate and ubiquinol 1 oxidation and generate a H+ electrochemical gradient similar to that observed in membrane vesicles. The only component between D-lactate dehydrogenase or ubiquinol and oxygen in the membranes that is directly involved in the generation of the H+ electrochemical gradient is cytochrome 0 | Escherichia coli |