Abstract
R(+)~thioctic acid is the naturally occurring cofactor in a-ketoacid, dehydrogenases. We show both photometrically by NADH + H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH +H2 catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. The racemate exhibits approximately 40% activity as compared to the R(+) form while the S(-) enantiomer photometrically shows little activity and yields no detectable reduced lipoic, acid.
Original language | English |
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Pages (from-to) | 691-692 |
Number of pages | 2 |
Journal | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
Volume | 49 |
Issue number | 9-10 |
DOIs | |
State | Published - Oct 1994 |
Keywords
- Diaphorase
- Lipoic Acid
- Stereospecificity
- Thioctic Acid