The oxidation of l(−)α-hydroxyglutaric acid in animal tissues

Abstract

1([long dash]) [alpha]-Hydroxyglutaric acid was oxidized to a-ketoglutaric acid by a dehydrogenase which was found in many animal tissues, especially in heart and kidney. The properties of this enzyme were studied in detail. Its action did not depend upon any coenzyme. A carrier was necessary for the reaction with molecular O; pyocyanine and a few closely related phenazine derivatives were found most active, whereas cytochrome C was inactive. H2O2 was formed during the reaction with O and was demonstrated in presence of cyanide. The enzyme action was reversible. Direct measurement of the potential was not possible. The optical iso-meride, d( + )[lalpah]-hydroxyglutaric acid, was not attacked by the dehydrogenase.