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- Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.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.Cytochrome oxidase and succinate-CoQ oxidoreductase are isolated from mitochondria and are incubated inthe presence of oxygen, along with cytochrome c, coenzyme Q,and succinate. What is the overall oxidation–reduction reactionthat can be expected to take place?
- The enzyme that catalyzes reaction below can be classified as: CoO COO NAD+ NADH + H* Но- | malate -C- H-Ć- dehydrogenase Охaloacetate Malate isomerase lyase hydrolase oxidoreductase ligase transferaseSome anaerobic prokaryotes reduce elemental sulfur to H2S. Assuming 100% efficiency, how much ATP could be synthesized by the oxidation of acetate by S under standard conditions?Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu
- The comparison of the active site geometries of chymotrypsin and subtilisin under the assumption that their similarities have catalytic signifi cance has led to greater mechanistic understanding of both these enzymes. Discuss the validity of this strategy.In steroid synthesis, squalene is oxidizedto squalene epoxide. This reaction is somewhat unusual, in thatboth a reducing agent (NADPH) and an oxidizing agent (O2) arerequired. Why are both needed?The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a phosphorylatedenzyme intermediate. If 3-phosphoglycerate is radioactively labeledwith 32P, the product of the reaction, 2-phosphoglycerate, does nothave any radioactive label. Design a mechanism to explain these facts.
- Because of the position of arsenic in the periodic table, arsenate (AsO43- ) is chemically similar to inorganic phosphate and is used by phosphaterequiring enzymes as an alternative substrate. Organic arsenates are quite unstable, however, and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.NH3 H-SCO A LES NH CH₂ NH CH₂ CH₂ 3 H-SCO A H3C SCO A 5. Describe the role of His in the catalytic mechanism shown.A histidine residue in the active site of aspartate transcarbamoylase is thought to be important in stabilizing the transition state of the bound substrates. Predict the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pHactivity profile of the enzyme.