Questions to study.
1. Enzymes as protein catalysts. Similarities and differences between enzymes and non-protein catalysts.
2. Structure of enzymes.
3. Coenzymes and prosthetic groups. Classification of coenzymes: vitamin and non-vitamin coenzymes.
4. Structure of the active site of enzymes. Functional groups of active site and their functions in enzymatic catalysis.
5. Mechanisms of enzyme-catalyzed reactions. Energy barrier of chemical reaction. Formation of enzyme-substrate complex. Possible ways of substrate molecule energizing to reach a transition state. Steps of enzyme-catalyzed reaction.
6. Kinetics of enzyme-catalyzed reactions. Dependence between the rate of enzyme-catalyzed reaction and substrate concentration. Physical essence of values of Km and Vмах. Michaelis-Menten equation.
7. Dependence between the velocity of enzyme-catalyzed reactions and pH and temperature.
8. Substrate specificity of enzymes. Types of substrate specificity.
9. Classification and nomenclature of enzymes. Characteristics of individual classes of enzymes.
10. Regulation of enzyme activity. Activators and inhibitors.
11. Types of inhibition. Irreversible inhibition. Suicide inactivators.
12. Reversible inhibition.
13. Other pathways of enzyme regulation: covalent modification - phosphorylation, restricted proteolysis, protein-protein interaction.
14. Allosteric enzymes. Features of allosteric enzyme structure. Mechanism of allosteric regulation. Significance of allosteric enzymes.
15. Isozymes and their uses in medicine.
16. Approaches to determining enzyme activity. Expression of enzyme activity.
17. Using enzymes in medicine.
18. Immobolized enzymes and their uses in medicine.
TESTS TO ASSESS FORMATION OF THE FOLLOWING COMPETENCIES: GC-1, GPC-1, 7, 9, PC-5, 12