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- Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activationIn an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
- An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? ExplainAn enzyme is discovered that catalyzes the chemical reaction A team of motivated researchers sets out to study the enzyme, which they callhappyase. They find that the kcat for happyase is 600 s−1 and carry out several additional experiments.When [Et] = 20 nM and [SAD] = 40 μM, the reaction velocity, V0, is 9.6μM s−1. Calculate Km for the substrate SAD.
- 1 what is does the induced -fit model account for? 2 why are most enzyme inactive at higher temperature ( greater than 37degree Celsius) 3 Does this happen to all enzymes in all species? 4 What are the formulas for the reduced form of the coenzymes?1. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 2. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?1) Biochemists use and define a standard transformed Free Energy (ΔG’o), what is all this notation stuff about anyway? 2) What is the mathematical relationship between ΔG’º and K’eq ? 3) What is the single biggest driver of the observed Keq ?
- 2 The free energy-requiring step in the synthesis of ATP is not the formation of ATP from ADP and Pi (ΔG ≈ 0), but the release of tightly bound ATP. Explain why this is not inconsistent with the +30.5 kJ⋅mol-1 free energy of formation of ATP in solution.5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a4 In a reaction system, the concentrations of Enzyme-Substrate complex (ES), free enzyme [E] and free substrate [S] are 5mM, 2mM and 45 mM respectively. If the enzyme has 5 identical binding sites for this substrate, then calculate the value of Equilibrium Association constant (Ka)