1. Describe the common characteristic among the reactions catalyzed by pyruvate dehydrogenase (PDH), isocitrate dehydrogenase (ID), and alpha-ketoglutarate dehydrogenase (KD) based on reversibility.
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![1. Describe the common characteristic among the reactions
catalyzed by pyruvate dehydrogenase (PDH), isocitrate
dehydrogenase (ID), and alpha-ketoglutarate
dehydrogenase (KD) based on reversibility.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F99a780b3-9d06-43f2-a31a-642fe8105020%2F0f94bafc-6c57-4b64-bdc3-76529a6e9602%2F4cq0whm.jpeg&w=3840&q=75)
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- 2. (a) ( In contrast to the pyruvate dehydrogen- ase complex, the a-ketoglutarate dehydrogenase (aKGDH) complex is not up- or downregulated by phosphorylation or dephosphorylation. However, the complex exhibits cooperativity modulated by the presence of ADP, ATP, inorganic phosphate (Pi), and Ca2+, as illustrated by the diagram on the right for the bovine kidney enzyme complex. Note in the diagram how the addition of 10 μM Ca2+ shifts the affinity of the enzyme complex for aKG from 20 mM Pi/-Ca2+ to 20 mM Pi/+Ca2+. Calcium especially en- hances the cooperative influence of ADP and ATP. Using the expanded copy of the diagram at the end of the problem set, estimate the change in S0.5 (re- member that for allosteric enzymes S0.5 corresponds to KM of a nonallosteric enzyme) for the enzyme complex in the presence of 20 mM Pi/-Ca2+ and in the presence of 20 mM Pi/+Ca2+. Compare similarly the change in S0.5 for the enzyme in the presence of 20 mM Pi/-Ca2+ plus 1.6 mM ADP to the enzyme in the…In own words, give 5 or more reasons why most of the clinical features of the diseases a-ketoglutarate dehydrogenase deficiency, succinate dehydrogenase deficiency, and fumarase deficiency involve muscle and nerve tissue? and explain those reasons.Because dichloroacetate inhibits the enzyme pyruvatedehydrogenase kinase, this compound has been used,with limited results, to treat lactic acidosis. The phosphorylation of the a-subunit of the pyruvate dehydrogenasecomponent of the pyruvate dehydrogenase complex bypyruvate dehydrogenase kinase causes complete loss ofenzymatic activity. Describe the theory behind the clinicaluse of dichloroacetate.
- In own words, give 5 or more reasons why most of the clinical features of the diseases a-ketoglutarate dehydrogenase deficiency, succinate dehydrogenase deficiency, and fumarase deficiency involve muscle and nerve tissue? and explain those reasons. Cite used references.. Briefly describe the biological rationale for cach of the following allosteric phenomena: (a) activation of pyruvate carboxylase by acetyl-CoA; (b) acti- vation of pyruvate dehydrogenase kinase by NADH; (c) inhibition of isoci- trate dehydrogenase by NADH; (d) activation of isocitrate dehydrogenase by ADP; (e) inhibition of a-ketoglutarate dehydrogenase by succinyl-CoA; (f) activation of pyruvate dehydrogenase phosphatase by Ca*.. Identify the Krebs cycle enzyme which acts on a five-carbon substrate, produces a four-carbon product substituent (attached to coenzyme A), and generates one molecule of NADH. a-ketoglutarate dehydrogenase pyruvate dehydrogenase citrate synthase malate dehydrogenase succinate dehydrogenase Which of the following enzymes consumes one molecule of NADH, during anaerobic fermentation in yeast, as it converts a two-carbon substrate molecule into a two-carbon product molecule? succinate dehydrogenase pyruvate decarboxylase C. isocitrate dehydrogenase lactate dehydrogenase alcohol dehydrogenase
- 7) What are the major pathways of glucose utilizations that are vary with physiological conditions, and organisms? (Describe the three possible fates of pyruvate) .Briefly describe the dual role of lipoic acid in the pyruvate dehydrogenase complex(i) When there is a deficiency of thiamine, blood levels of pyruvate and a- ketoglutarate increase, especially after a high-glucose meal . Explain the observations mentioned. (ii) Explain how El of pyruvate dehydrogenase complex is regulated using covalent modification
- a) describe the overall reaction catalyzed by the pyruvate dehydrogenase Situational Problems I. Oxidative decarboxylation of pyruvate and the TCA cycle in muscles are stimulated by increased aerobic excrcise. These processes operate only when O, is present, although oxygen does not participate directly in these processes. Explain why oxidative decarboxylation of pyruvate is activated under aerobic conditions. For the answer: a) describe the overall reaction catalyzed by the pyruvate complex (PDH) and its regulation; b) outline the intermediates and enzymes of the TCA cycle; c) explain the relationship between the reactions of PDH and the TCA cycle and the respiratory chain.25) Write down the two gluconeogenic reactions that allow the glycolytic enzymes hexokinase and phosphofructokinase to be bypassed (Describe the effects of (1) oligomycin and (2) uncouplers of oxidative phosphorylation, e.g., dinitrophenol (DNP), carbonyl cyanide-p- trifluoromethoxyphenylhydrazone (FCCP), on respiration and ATP synthesis when added to a suspension of mitochondria with excess malate, ADP, and inorganic phosphate (Pi).
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