

Author: Lanterman Margaret M. Dickinson J. Richard Danner Dean J.
Publisher: Oxford University Press
ISSN: 1460-2083
Source: Human Molecular Genetics, Vol.5, Iss.10, 1996-10, pp. : 1643-1648
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Abstract
Dihydrolipoamide dehydrogenase is a common component of mammalian multienzyme complexes that decarboxylate α-ketoacids and catabolize glycine. The common function is to reoxidize a reduced lipoate component of each complex, thereby preparing that lipoate for another round of catalysis. Regions within dihydrolipoamide dehydrogenase involved in association with other proteins of the complexes are poorly defined, and despite high amino acid sequence conservation through evolution, it is unknown if dihydro-lipoamide dehydrogenases are functionally equivalent across species. To address this issue, we asked whether the human enzyme could restore function to the -ketoacid dehydrogenase complexes in a yeast strain deficient in endogenous dihydrolipoamide dehydro-genase. This dihydrolipoamide dehydrogenase null mutant will not grow on non-fermentable carbon sources. The human enzyme expressed from a
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