5 Catalytic Proteins-Enzymes
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After reading this chapter you should be able to:
- Describe the characteristics of enzymatic reactions from the viewpoint of free energy, equilibrium, kinetics and direction of the reactions in comparison with simple chemical reactions.
- Discuss the structure and composition of enzymes, including cofactors, and conditions that affect enzymatic reactions.
- Describe enzyme kinetics based on the Michaelis-Menten equation and the significance of the Michaelis constant (Km).
- Describe the elements of enzyme structure that explain their substrate specificity and catalytic activity.
- Describe regulatory mechanisms affecting enzymatic reactions, including regulation by allosteric effectors and covalent modification.
- Differentiate among the three types of enzyme inhibition from the viewpoint of enzyme kinetics.
- Discuss the therapeutic use of enzyme inhibitors and the diagnostic utility of clinical enzyme assays.
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