1.1.5.10: D-2-hydroxyacid dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about D-2-hydroxyacid dehydrogenase (quinone), go to the full flat file.
Reaction
Synonyms
(R)-2-hydroxy acid dehydrogenase, (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase, D-lactate dehydrogenase, DLD, Fe-S D-iLDH, lldE, NAD-independent D-lactate dehydrogenase
ECTree
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Cofactor
Cofactor on EC 1.1.5.10 - D-2-hydroxyacid dehydrogenase (quinone)
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Fe-S center
the enzyme contains an Fe-S oxidoreductase domain. The Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by the enzyme (Fe-S D-iLDH), and it helps the enzyme associate with the cell membrane
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the purified enzyme has a spectrum typical of a flavoprotein. The change induced in the spectrum on addition of D-malate or D-lactate suggests the formation of a flavin semiquinone. Flavin can be removed by treatment with acid ammonium sulfate, and activity can be restored to the inactive apoenzyme by addition of FAD, but not of FMN or riboflavin
FAD
the enzyme contains a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely loses the ability to use coenzyme Q10. The FAD containing dehydrogenase domain is no longer associated with the cell membrane, and it can not support the utilization of D-lactate as a carbon source