Pyruvate dehydrogenase catalyzes the conversion of pyruvate to acetyl CoA. In this reaction, one molecule each of the catalytic coenzymes TPP, FAD and lipoamide participate in the reaction but are not consumed. OTrue O False
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Pyruvate dehydrogenase catalyzes the conversion of pyruvate to acetyl CoA. In this reaction, one molecule each of the catalytic coenzymes TPP, FAD and lipoamide participate in the reaction but are not consumed.
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- Ethanol as a Source of Metabolic Energy (Integrates with Chapters 19 and 20.) Acetate produced in ethanol metabolism can be transformed into acetyl-COA by the acetyl thiokinase reaction: Acetate+ATP+CoASHacetyleCoA+AMP+PPiAcetyle-CoA then can enter the citric acid cycle and undergo oxidation to 2 CO2by this route, assuming oxidative phosphorylation is part of the process? (Assume all reactions prior to acetyl-CoA entering the citric acid cycle occur outside the mitochondrion). Per carbon atom, which is a better metabolic fuel, ethanol or glucose? That is, how many ATP equivalents per carbon atom are generated by combustion of glucose versus ethanol to CO2?Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
- The Effect of lodoacetic Acid on the Glyceraldehyde-3-P Dehydrogenase Reaction (Integrates with Chapters 4 and 14.) How might iodoacetic acid affect the glyceraldehydes-3-phosphate dehydrogenase reaction in glycolysis? Justify your answer.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.Identify the Krebs cycle enzyme that consumes a 3-carbon substrate molecule, producing a 2- carbon product molecule (attached to acetyl-CoA), along with NADH, and one molecule of CO2. succinyl CoA synthetase a-ketoglutarate dehydrogenase pyruvate dehydrogenase isocitrate dehydrogenase malate dehydrogenase
- Which enzyme is used for both the synthesis and breakdown of acetoacetate? thiolase O HMG-CoA synthase OB-hydroxybutyrate dehydrogenase O B-Ketoacyl-CoA transferaseIn beta-oxidation, which cofactor is required the for second oxidation reaction (conversion of beta-hydroxyacyl-CoA to beta-ketoacyl-CoA)? NAD+ water FAD CoA-SHIn the pyruvae dehydrogensae complex, acetyl-coa is released by the dihydrolipoyl transacetylase activity. What is the purpose of the following enzymatic activity.
- A patient exhibiting all the symptoms of beriberi is placed on a thiamine-enriched diet; however, the symptoms do not disappear. Genetic screening suggests a defect in pyruvate dehydrogenase phosphatase. Briefly explain why the genetic defect caused beriberi symptoms andy why thiamine supplementation had no effect.Coenzyme A (CoA-SH) plays an important role in the Pyruvate Dehydrogenase Complex reaction. Which is correct? Coenzyme A serves as an electron acceptor in this reaction. The hydrolysis of a CoA thioester has a positive AG", the hydrolysis is endergonic and unfavorable. Coenzyme A is derived from thiamine, a vitamin. Coenzyme A contains -SH group and can serve as an acyl group carrier.Upon considering the complete oxidation of one mole of fatty acyl (CoA) of an arachidic acid (20:0). Answer the following lettersa. total no. of NADH produced from the oxidation of all acetyl CoA in the acetyl cycleb. otal no. of FADH2 produced from the oxidation of all acetyl CoA in the acetyl cyclec. total atp yield