Dihydrolipoamide dehydrogenase - Open Access .click

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Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts

Planta, 1996
Two distinct dihydrolipoamide dehydrogenases (E3s, EC 1.8.1.4) have been detected in pea (Pisum sativum L. cv. Little Marvel) leaf extracts and purified to at or near homogeneity. The major enzyme, a homodimer with an apparent subunit M(r) value 56,000 (80-90% of overall activity), corresponded to the mitochondrial isoform studied previously, as ...
Tino Krell, Lindsay Jg, Conner M
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Dihydrolipoamide dehydrogenase: a ‘new’ function for an old enzyme? [PDF]

Biochemical Society Transactions, 1988
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Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.

Journal of biochemical and pharmacological research
Dihydrolipoamide dehydrogenase (DLDH) is a multifunctional oxidoreductase and is well known as an essential component of four mammalian mitochondrial multienzyme complexes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched chain α-keto acid dehydrogenase, and the glycine cleavage system. However, existence of extracellular DLDH in mammals,
Liang-Jun, Yan +3 more
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Thioredoxin reductase and dihydrolipoamide dehydrogenases of Plasmodium falciparum

2006
Plasmodium falciparum is an obligate intracellular protozoan parasite and is the causative agent of malaria, which infects 270 million people and causes 2-3 million human deaths each year. During the erythrocytic stages of their life cycle the parasites are exposed to reactive oxygen species generated by the host and their own metabolism.
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Dihydrolipoamide dehydrogenase and lipoic acid in Trypanosoma brucei