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Results 1 - 3 of 3
EC Number
General Information
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
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
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
Results 1 - 3 of 3