. 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*.
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- Study Figure 19.18 and decide which of the following statements is false. Pyruvate dehydrogenase is inhibited by· NIADH. Pyruvate dehydrogenase is inhibited by AΤΡ. Citrate synthase is inhibited by NADH. Succinyl-CoA activates citrate synthase. Acetyl-CoA activates pyruvate carboxylase.Briefly describe the biological rationale for each of the following allosteric phenomena: (a) activation of pyruvate carboxylase by acetyl-CoA; (b) activation of pyruvate dehydrogenase kinase by NADH; (c) inhibition of isocitrate 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 Ca2+.Briefly describe the biological rationale for each of the following allosteric phenomena: (a) activation of pyruvate carboxylase by acetyl-CoA; (b) activation of pyruvate dehydrogenase kinase by NADH; (c) inhibition of isocitrate dehydrogenase by NADH; (d) activation of isocitrate dehydrogenase by ADP; (e) inhibition of α-ketoglutarate dehydrogenase by succinyl-CoA; (f) activation of pyruvate dehydrogenase phosphatase by Ca2 +.
- 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…Remembering that the Pyruvate dehydrogenase complex and the alpha ketoglugarate complex catalyze similar reactions, please match the following terms with its description: Dihydrolipoyl dehydrogenase (E3) 1) an alpha-keto acid that undergoes oxidative decarboxylation 2) is analogous to the pyruvate dehydrogenase reaction in which there's an oxidative decarboxylation with a concomitant formation of an acyl-CoA thioester 3) is analogous to the pyruvate dehydrogenase reaction and the isocitrate dehydrogenase reaction in which there's an oxidative decarboxylation with a concomitant formation of an acyl-CoA thioester 4) catalyzes the oxidative decarboxylation of alpha ketoglutarate 5) regenerates active dihydrolipoyl transacetylase (E2) 6) catalyzes the oxidative decarboxylation of succinyl coa 7) catalyzes the oxidative decarboxylation of alpha isocitrate 8) catalyzes the formation of Succinyl CoA Alpha ketoglutarate The alpha ketoglutarate dehydrogenase complex Alpha ketoglutarate…(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
- Catalytic mechanism of the Pyruvate Dehydrogenase Complex Match the following coenzymes with the type of reaction or catalytic steps they are associated with during the catalysis of Pyruvate transformation into Acetyl-CoA by the Pyruvate Dehydrogenase Complex: NAD+ V [Choose] formation of a low energy thioester bond decarboxylation TPP oxidation/reduction formation of a high energy thioester bond Coenzyme A [ Choose ] Lipoyl Lysine [ Choose ] FAD [ Choose ]Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?How detailed is the enzyme structure known below(It's Pyruvate Dehydrogenase )? What insight(s) does this structural detail give you about the enzyme mechanism.The mechanism for the conversion from alpha kytoglutarate into succinyl CoA by alpha-ketoglutare dehydrogenase is analogous to the pyruvate dehydrogenase mechanism. Draw and show the major intermediates and arrow pushing for the enzyme-catalyze process for the conversion of alpha-ketoglutarate to succinyl CoA. Note: the carbanion of thiamine pyrophosphate nucleophillically attacks C-2 of the alpha-ketoglutarate, i.e., the carbonyl carbon of that substrate.
- Describe the common characteristic among the reactions catalyzed by pyruvate dehydrogenase (PDH), isocitrate dehydrogenase (ID), and alpha-ketoglutarate dehydrogenase (KD) based on reversibility.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.Draw a plausible mechanism for the oxidation of dihydrolipoamide to lipoamide by the E3 subunit (dihydrolipoamide dehydrogenase) of pyruvate dehydrogenase complex.