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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.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.
- 1. What is the difference between the lock and key model in the induced fit model enzyme-substrate binding? 1a. What factors affect an enzymes catalytic function?1. A. Estimate from the graph what the Vmax is for the enzyme without inhibitor present (black circles) and in the presence of the inhibitor (green squares). B. Estimate the Km from the graph without inhibitor present (black circles) and in the presence of the inhibitor (green squares). C. Based on the data, what type of reversible inhibitor do you think was used? Explain your answer.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
- 1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?1. There are two major categories of enzyme, inhibition, name, and describe them.  1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?
- 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”?1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
