EC Number   |
General Information |
Reference |
|---|
  1.1.5.12 | metabolism |
the isolated FAD-containing dehydrogenase domain retains 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S D-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely lost the ability to use coenzyme Q10. The Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S D-iLDH, and it helps the enzyme associate with the cell membrane |
761384 |
| 1.1.5.12 | 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 |
-, 740030 |
| 1.1.5.12 | physiological function |
inactivation of Dld results in the loss of the ability to grow with D-lactate. Heterologous expression in Corynebacterium efficiens enables this species to grow with D-lactate as sole carbon source |
-, 727253 |
