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Showing 1 to 8 of 8 for “"2-oxoglutarate dehydrogenase"”.
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Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex: e1 and e2 substrate specificty, e1 carboligase activity, and e2 interchain succinyl transfer
Escherichia coli (E. coli) 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc) contains three components: a thiamin di phosphate (ThD P) dependent 2-oxogl utarate dehydrogenase (E1 o), a di hydrol i poylsucci nyl transferase (E2o), and a di hydrol i poyl dehydrogenase (E3). The first two …
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Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli
… cofactor essential for the activity of 2-oxoacid dehydrogenases and the glycine cleavage system. In the absence of lipoic acid modification the dehydrogenases are inactive and aerobic metabolism is blocked. In Escherichia coli two pathways for the attachment of lipoic acid exist, a de novo …
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The growth, physiology and intermediary metabolism of bacillus stearothermophilus.
… of all the TCA cycle enzymes including the 2-oxoglutarate dehydrogenase system were present. The activity of this enzyme complex could not be detected when the bacterium was grown on glucose. B. stearothermophilus PS2 growing at 55 °C could be thermoadapted to grow at 37 °C. The pathways of …
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The role of ABHD11 in the regulation of the hypoxia inducible transcription factors
… members of a diverse group of enzymes termed 2-oxoglutarate-dependent dioxygenases. These enzymes all require oxygen, iron and the Tricarboxylic Acid (TCA) cycle metabolite, 2-oxoglutarate (2-OG/a-ketoglutarate) for catalytic activity. Therefore, understanding how 2-OG levels are regulated is …
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Xylitol Production From D-Xylose by Facultative Anaerobic Bacteria
… the difference in xylose reductase and xylitol dehydrogenase activity was highest at 24 h, whereas for cell cultures that were grown in gluconate and xylose, the difference in the reductase and dehydrogenase activities was highest at 12 h after xylose addition. The NAD+ dependent xylitol …
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Immunological and biosynthetic studies of the human pyruvate dehydrogenase complex
The human pyruvate dehydrogenase multi-enzyme complex (PDC) catalyses the oxidative decarboxylation of pyruvate, transferring the resultant acetyl group to coenzyme A. It belongs to the family of 2-oxoacid dehydrogenase complexes that includes the 2-oxoglutarate dehydrogenase (OGDC) and …
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Structure and Molecular Biology of the Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus
The pyruvate dehydrogenase multienzyme complex (PDHC) from the thennophilic, Gram-positive bacterium Bacillus stearothermophilus is assembled around a core of 60 copies of the dihydrolipoamide acetyltransferase (E2p) component, organized with icosahedral symmetry. The peripheral subunits, attached …
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Analysis of genetic mutations using a recombinant model of the mammalian pyruvate dehydrogenase complex
The human mitochondrial pyruvate dehydrogenase complex (PDC) is a vital metabolic assembly that controls the key committed step in aerobic carbohydrate utilisation and energy production and as such is responsible for overall glucose homeostasis in man. PDC, particularly from prokaryotic sources, …