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The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors.
ordered mechanism, first D-lactate and then 2,6-dichlorophenol-indophenol bind to the enzyme to form a ternary complex, from which pyruvate and reduced 2,6-dichlorophenol-indophenol dissociate in that oder
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