The pyruvate and alpha-ketoglutarate dehydrogenase complexes isolated from pig heart mitochondria promote the reduction of thioredoxin in the presence of their alpha-ketoacid substrates, coenzyme A, and free lipoate. Substrate-specific generation of reduced thioredoxin was established by two independent methods, viz. reduction of insulin and thioredoxin reductase-catalyzed NADPH formation. Dihydrolipoate accumulating in the absence of NAD+ is the likely intermediate. A redox function in alpha-ketoacid oxidation provides a potential role for the specific thioredoxins previously identified by us in mitochondria.
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UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110
CHACIN, J
HARRIS, JB
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UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110
HARRIS, JB
ALONSO, D
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UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110UNIV CALIF SAN FRANCISCO,SAN FRANCISCO GEN HOSP,GASTROENTEROL RES LAB,SAN FRANCISCO,CA 94110