2. How is a "committed step" defined in the context of a metabolic pathway and why are they important? Which steps and/or enzymes are involved in the committed steps in the Krebs Cycle? What are the possible implications of these steps were deregulated?
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- 7. To what main enzyme class do the enzymes that catalyze the following reaction belong? (Oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) со о 8. Label the following as examples of a "lock and key" model or an "induced fit" enzyme model? substrate a. b. tive sihe a. b. yme-bstrate comples1. A metabolic pathway proceeds according to the scheme, R → S →T→U→ V→ W. A regulatory enzyme, X, catalyzes the first reaction in the pathway. Which of the following is most likely correct for this pathway? A) Either metabolite U or V is likely to be a positive modulator, increasing the activity of X. B) The first product S, is probably the primary negative modulator of X, leading to feedback inhibition. C) The last product, W, is likely to be a negative modulator of X, leading to feedback inhibition. D) The last product, W, is likely to be a positive modulator, increasing the activity of Х. E) The last reaction will be catalyzed by a second regulatory enzyme.Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
- 7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)5. Gout can be caused by superactivation of PRPP synthase, or partial deficiency of hypoxanthine-guanine phosphoribosyl transferase. Why the change in these enzyme activities can induce the development of this disorder? For the answer: a) write down the scheme of the reactions catalyzed by these enzymes;b) specify metabolic pathways these reactions take part in; c) answer the main question of the problem.1. What are at least 2 factors that affect rate of a reaction within a metabolic pathway? Define and explain these and provide at least one example for each.
- 7. As far as location, where do each of these metabolic reactions occur in a eukaryote? A prokaryote? Why the difference?1. For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: ES k, and k,' ES à E and P k,. E + S a. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E, – ES. (If you have difficulty in doing it, please consult lecture note) b. Assume K = 0.038 mol.L' at 25 °C, when the substrate concentration is 0.156 Mol.L', the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.8. Structures of three coenzymes involved in Phase II conjugation reactions are shown below. For each coenzyme, circle the portion of the coenzyme that is transferred during metabolic reaction. NH, CH NH, COO CH, H2C OH CH НО O-UDP HC H H ОН он он UDP-Glucuronate S-Adenosylmethionine (S-AdoMet) SCo AcetylSCo
- 3. How does an enzyme work? (A) Use 3 different colors to color the coding circles and corresponding structures in the figure. (B) Beneath steps 1-3, briefly explain, in your own words, what is happening. 2omysna Ju2io atauoon eu8 3 arit to HA slie EUSAwee se pAbiceph opnyn brorejue Ap su sAG ylsteo of so beeu + uboig s ot slsuas s chrdsetisoinorco O Enzyme O Reactant(s) O Product(s) in resiscpepnselifsa op mm Delits nogieadA noteeguoima fnotlengede bns noltesplb noewied eaneiellib or సూగాత6. Reciprocal regulation of opposing pathways is necessary to avoid the wasteful synthesis anddegradation of metabolic intermediates. Provide two distinct examples of reciprocal regulation. Bespecific, and be sure to explain the conditions that signal enzyme activation and/or inhibition.23. With the aid of a diagrams describe the Krebs cycle in full detail.