Bke2 Biochemistry Exercises
Group exercise: Mechanisms of enzyme regulation
- Why is regulation important in biological systems. Discuss!
- Name as many different modes of regulation you can think of. Which type of modification of the protein is required in each case? Is the modification reversible or irreversible?
- Discuss and try to explain allostery. Allostery can be homotropic or heterotropic. Explain. What does positive cooperativity mean? Which glycolytic enzymes are allosterically regulated, and how?
- If you separated hemoglobin into dimers of (a+b) subunits, would you expect the dimers to bind more or less O2 at low O2 tensions? Explain. What effect would 2,3-bisphosphoglycerate have on oxygen binding?
- What does the curve for the dependence of the reaction velocity on the substrate concentration for an allostrically controlled enzyme look like? Do these enzymes follow Michaelis-Menten kinetics?
- Explain the term feedback control. Why is it necessary?
- Discuss the details of proteolytic activation. What may be the reasons for using protelytic cleavage as the means to control e.g. blood clotting and digestive enzymes?
Reading material: Horton chapters 4.13 5.10 6.8 9.12 10.2 11.5 12.6 13.3 13.7 17.20 18.2 18.7
Lectures:
Mechanisms of enzyme regulation
Links:
Suggested answers
Exercise by Inger Andersson
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