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CHM 376 Biochemistry I Fall 2023 Problem Set 9D: Enzyme Regulation 1. Why is it necessary to regulate enzyme activity? 2. What is Abl kinase and how does the loss of Abl kinase affect the cell? What is Gleevac TM ? 3. How is enzyme activity regulated by gene expression and proteolysis ? 4. Explain (not just list) all the cellular mechanisms used to regulate enzyme activity. 5. What are the two ways enzymes are regulated by temperature ? 6. What is a temperature sensitive mutation. Give one example of a temperature sensitive mutation. Meow. 7. Why mammalian sperm production and storage carried out in an organ external to the main body cavity? 8. Draw the pH rate profile for an enzyme that has a single titratable amino acid at the active site, with a pK a of 4.2 that acts as a base. 9. Draw the pH rate profile for an enzyme that has a single titratable amino acid at the active site, with a pK a of 4.2 that acts as an acid. 10. Why is the pH rate profile of many enzymes shaped like a “ bell ”? 11. What is proteostasis? 12. Name several mechanisms involving irreversible covalent regulation of enzyme activity. In your answer, define the meaning of the terms (a) zymogen and (b) suicide inhibitor. 13. How is Disulfiram used in the treatment of alcoholism? What kind of inhibitor is disulfiram? 14. Provide one example by which enzyme activity is regulated by reversible covalent modification. In your answer, include definition for the kinase and phosphatase . 15. What is one common substrate of almost every kinase? What is one common substrate of almost every phosphatase? What is one common product of almost every phosphatase? 16. What is a consensus sequence? What role do these sequences play in regulating enzyme function?

17. What is the mechanism of the drug Sitagliptin? How does it produce similar effects as the drug Ozempic TM ? 18. What is the definition of the term surmountable as it relates to the study of enzymes. Why are competitive inhibitors surmountable? 19. Draw L-B plots for an enzyme-catalyzed reaction in (a) absence of an inhibitor; (b) presence of 3 separate concentrations of a competitive inhibitor; (c) 3 separate concentrations of an uncompetitive inhibitor and (d) 3 separate concentrations of a mixed inhibitor, in which the inhibitor binds better to E than to ES. 20. What is the difference between the binding of a competitive inhibitor and an allosteric inhibitor to an enzyme? Which type of inhibitor is surmountable , and why? 21. What class of inhibitors are transition state analogs ? What makes a transition state analog a potent inhibitor? 22. Why are transition state analogs useful tools for studying enzyme function? 23. What is autoinhibition . Explain one example of an enzyme that uses autoinhibition. 24. Explain the concept of product inhibition and feedback inhibition . What is the significant difference between the chemical structure of a product inhibitor and a feedback inhibitor? 25. Name and describe the binding locations and mechanisms of the positive and negative allosteric regulators of the enzyme Aspartate Transcarbamoylase. Why is this an example of feedback inhibition, and how does it benefit the cell. 26. How can one identify which enzyme is regulated in a multienzyme metabolic pathway? 27. The K M of the enzyme aldehyde dehydrogenase for ethanol is 30 m M. Due to a mutation, some individuals carry one or two copies of a rare allele in which the K M for ethanol is 700 m M. What are the physiological consequences of alcohol consumption for those individuals carrying rare mutant allele? 28. What is an isozyme? How are two (or more) distinct isozymes the same? What would differ between two different isozymes? Why do different cells (or tissues) have different isozymes? 29. What is the difference between an isozyme and an allozyme? 30. Explain the two modes of regulation of the enzyme Glycogen Phosphorylase, an enzyme that frees glucose molecules from storage. 31. Consider two distinct types of cells In cell type-1, an enzyme should always be converting a substrate into product, even at low substrate concentrations. In cell type-2, the substrate should only convert substrate into product when the substrate concentration is high. Explain

how cells can use isoenzymes to make this possible. Note that the answer does not involve allosteric effectors or post translational modifications to the enzyme. 32. Explain the concept of K M control.

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