The same E1-Ez-E3 multienzyme structure found in the pyruvate dehydro- genase and the a-ketoglutarate dehydrogenase complexes is also used in the branched-chain a-ketoacid dehydrogenase complex, which participates in the catabolism of branched chain amino acids. Draw the reaction product when the following substrate is acted on by the branched chain a-keto acid dehydrogenase complex. H,C -C-COo- H,C
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- 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.Complete oxidation of a 16-carbon fatty acid can yield 129 molecules of ATP Study Figure 19.2 and determine how many ATP molecules would be generated if a 16-carbon fatly acid were metabolized solely by the TCA cycle, in the form of S acetyl-CoA molecules.A Deficiency on 3-Phosphogtycerate Dehydrogenase Can Affect Amino Acid Metabolism Although serine is a nonessential amino acid, serine deficiency syndrome has been observed in humans. One such form of the syndrome is traceable to a deficiency in 3-phosphoglycerate dehydrogenase (see Figure 25.31). Individuals with this syndrome not only arc serine-deficient but also arc impaired in their ability to synthesize another common ammo acid, as well as a class of lipids. Describe why.
- Radiolabeling with 14C-Glutamate Describe the labeling pattern that would result from the introduction into the TCA cycle of glutamate labeled at Cy with 14C.The enzyme, dihydrolipoamide dehydrogenase is present in both pyruvate dehydrogenase complex and α-ketoglutarate dehydrogenase complex. What type of reaction is catalyzed by these complexes? Describe the role of dihydrolipoamide dehydrogenase in these reactions.For the pyruvate dehydrogenase complex, please identify the oxidation states of every atom and prove whether the reaction is oxidized or not Pyruvate --> Hydroxyethyl TPP B. Hydroexythl TPP --> Acetyl Lipoylysine C. Acetyl Lipoylysine --> Acetyl-CoA
- Which of the following is true about comparing the α-ketoglutarate dehydrogenase complex and the pyruvate dehydrogenase complex? Group of answer choices They catalyze reactions that produce the exact same set of products They are both dehydrogenase complexes, but have very different structures They both catalyze reactions that oxidize NADH to NAD+ They both use the same E3 enzyme component Which of the following best describes stage 2 of the citric acid cycle? Group of answer choices ATP production by the electron transport chain production of acetyl CoA regeneration of oxaloacetate release of 2 carbons as carbon dioxideIdentify 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 dehydrogenaseThe pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate to acetyl‑CoA and CO2.CO2. Multiple copies of pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3) along with five cofactors form the PDH complex. Biochemists have studied the PDH complex for decades, in part due to its interesting use of substrate channeling during catalysis. What is the benefit of substrate channeling? A. Intermediates of a multistep reaction sequence do not dissociate from the enzyme complex. B. Every intermediate or product made by the PDH complex enters the citric acid cycle as a substrate. C. The PDH complex sequesters excess substrate to use at later time. D. Reaction progress is not limited by the diffusion constant. E.The PDH active site forms in the hydrophobic core of the complex instead of a surface‑exposed region.
- The pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate to acetyl‑CoA and CO2.CO2. Multiple copies of pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3) along with five cofactors form the PDH complex. Biochemists have studied the PDH complex for decades, in part due to its interesting use of substrate channeling during catalysis. What is the molecular mechanism of substrate channeling in the PDH complex? A. The swinging lipoyllysyl arm of E2 carries electrons and an acetyl group from E1 to E2. B.The active sites of E1, E2, and E3 undergo conformational changes that move products of one reaction to their next position without solvent exposure. C.Electrons and an acetyl group travel between E1 and E2 through a tunnel in E2. D. Metal ions coordinated with thiamine pyrophosphate (TPP) in E1 shield the electrons and acetyl group from scavenging by other enzymes until they reach E3.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.What are the similarities and differences between the reactions catalyzed by pyruvate dehydrogenase and a-ketoglutarate dehydrogenase?