Results 171 to 180 of about 10,826 (186)
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Thermally Induced Disintegration of theBacillus stearothermophilusDihydrolipoamide Dehydrogenase

Bioscience, Biotechnology, and Biochemistry, 2000
Upon heat treatment of the pyruvate dehydrogenase complex from Bacillus stearothermophilus, the most thermostable component is a dihydrolipoamide dehydrogenase (E3c). To understand this stability, the thermal disintegration of E3 dissociated from the complex (E3d) was examined, comparing with that of E3c. Judging from residual activity and inactivation
Y, Hiromasa   +3 more
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The cDNA encoding canine dihydrolipoamide dehydrogenase contains multiple termination signals

Gene, 1995
A 2288-bp cDNA sequence encoding dihydrolipoamide dehydrogenase (DLDH; dihydrolipoamide: NAD+ oxido-reductase; EC 1.8.1.4) was obtained by isolating a 1762-bp cDNA clone from a canine skeletal muscle library in the vector, lambda UNIZAP, combined with PCR amplification of the 5' end of the mRNA.
A S, Martins   +3 more
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Dihydrolipoamide dehydrogenase from Leishmania donovani: New insights through biochemical characterization

International Journal of Biological Macromolecules, 2018
Dihydrolipoamide dehydrogenase (DLDH) regulates many crucial metabolic pathways as a multi-enzyme complex. Leishmania donovani dihydrolipoamide dehydrogenase (LdDLDH) has two variants present on two different chromosomes with very less sequence similarities. In the current study, we cloned both the variants in pET28a (+) vector and expressed in Rosetta-
Adarsh Kumar, Chiranjivi   +1 more
openaire   +2 more sources

Biochemical characterisation of dihydrolipoamide dehydrogenase from potato

1995
Dihydrolipoamide dehydrogenase (E3), a member of the group of Flavin-containing pyridine nucleotide-disulphide oxidoreductases, exists as a homodimer containing 1 Flavin adenine dinucleotide (FAD) per subunit and a redox-active disulphide. Dihydrolipoamide dehydrogenase is also an integral component of the 2-oxoacid dehydrogenase complexes and the ...
openaire   +2 more sources

Lipoic Acid and Dihydrolipoamide Dehydrogenase in Halophilic Archaeobacteria

1991
We have discovered the presence of dihydrolipoamide dehydrogenase (DHLipDH) in the halophilic archaeobacteria, despite the fact that these organisms lack the multienzyme complexes with which this enzyme is associated in eubacteria and eucaryotes. We will discuss (a) the discovery, purification and characterisation of the halophilic DHLipDH, (b) the ...
Michael J. Danson   +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.
openaire   +2 more sources

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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Dihydrolipoamide dehydrogenase

1994
D. Schomburg, M. Salzmann, D. Stephan
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[20] Dihydrolipoamide dehydrogenase: Activity assays

1995
Mulchand S. Patel   +2 more
openaire   +1 more source

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