knowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors, determine the nature of the inhibition by Astrozolamide and explain your reasoning! 100 No inhibitor Astrozolamide 0.2 0.4 0.6 0.8 (S) (mm) pre"A JO %) A
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- In 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.Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
- 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 activationThe energy released by the hydrolysis of ATP is primarily stored between the alpha and beta phosphates equal to -57 kcal/mol harnessed as heat energy by the cell to perform work providing energy to coupled reactions1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain
- 1. Can you describe how electrostatic and steric considerations may lead to preferential stabilization of the transition state at an enzyme active site? 2. What factors are involved in “transition-state complementarity”?6. 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.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? Explain
- 5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?4 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)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?