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- 1.Why do you think glutathione occurs in a concentration as high as glucose? 2.Explain why glutathione must be transported from cytosol to mitochondria. 3.Explain why glutathione can confer therapeutic benefit when taken orally.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.2. Which of the following statements is TRUE about phosphofructokinase-1? Select one: a. It is stimulated by AMP and ADP. b. It is inhibited by AMP and ADP. c. It is stimulated by citrate and ADP. d. It is stimulated by citrate and ATP.
- 1. Please identify the substrate and type of reaction, and explain how these reactions work for the following two enzymes Two enzymes: succinate dehydrogenase and L-amino acid reductase1. Why is the use of monosodium glutamate (MSG) highly debated?1. What is the significance of the different diameters of zones of inhibition?
- 10. Mention the Clinical Applications of Beta oxidation of fatty acids?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.9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
- 2. a. How do the majority of proteins that exist outside cells get outside cells? Explain the pathway. b. Explain at least three major exceptions to your answer in part a.1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?1. Describe the reaction catalyzed by salivary amylase. To which class of enzymes does amylase belong? Explain thoroughly.