7. How does enzyme inhibition occur? Give and illustrate the reaction between enzyme and substrate in the three types of enzyme inhibition.
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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 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 activationWhich 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.
- 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 pieces1. 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.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?1. Define optimum pH and temperature of an enzyme.2. How do changes in pH and temperature affect the native conformation of an enzyme?1. Compare and contrast the activation free energy and the free energy change for an enzyme-catalyzed reaction.
- 1. Using the following data, graph percent enzyme activity on the y-axis and pH on the x-axis 2.Do these enzymes have different optimum pHs? Explain why or why not. 3. Research what specific human enzymes would best match the data.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?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.
