(a) Lock and key model versus induced fit model of enzyme activity.
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(a) Lock and key model versus induced fit model of enzyme activity.
(b) Competitive and non-competitive enzyme inhibitors.
(c) Reversible and irreversible enzyme inhibitors.
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- Describe the induced-fit model of enzyme activity. *Explain how the following mechanisms regulate enzyme activity.(a) Covalent modification (b) Genetic control(c) Allosteric regulation (d) Feedback inhibitionRegarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
- The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.Characterization of enzyme activity does not allow us to: a. determine how different variables affect the enzyme's ability to function b. determine the molecular composition of the enzyme c. determine the optimal environment for an enzyme to function d. determine the effect of inhibitors on the enzyme
- “Induced fit” means that when a substrate binds to an enzyme’s active site, (a) it fits perfectly, like a key in a lock (b) the substrate and enzyme undergo conformational changes (c) a site other than the active site undergoes aconformational change (d) the substrate and the enzyme become irreversibly bound to each other (e) c and dPractice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of ReactionBased on some preliminary measurements, you suspect that a sample of enzyme contains an irreversible enzyme inhibitor. You decide to dilute the sample 100-fold and remeasure the enzyme’s activity. What would your results show if an irreversible inhibitor is present?
- a) What is the Steady State assumption; how does steady state differ from equilibrium? b) Transition state; what are two ways that enzymes can decrease the transition state energy?Which type of enzyme regulation is best for the following situations?(a) An enzyme that becomes overactive during a disease(b) An enzyme needed only when there is low blood glucose(c) An enzyme that springs into action when a traumatic injury occurs(d) An enzyme needed only during adolescenceDraw three different Lineweaver-Burke plots for an enzyme in the presence or absence of a (1) competitive inhibitor, (2) uncompetitive inhibitor, (3) noncompetitive inhibitor. Indicate on your graphs: Vmax, max (app), Km and Km (app) for each case.