Enzymes_Lecture_full detailed files.pptx

Enzyme

1. Enzymes Lecture Presentation

2. Introduction to Enzymes Biological catalysts that speed up reactions Mostly proteins, some RNA (ribozymes) Highly specific to substrates

3. Properties of Enzymes Increase reaction rate Lower activation energy Do not change equilibrium Reusable molecules

4. Structure of Enzymes Apoenzyme (protein part) Cofactors (metal ions, coenzymes) Holoenzyme = apoenzyme + cofactor

5. Active Site Region where substrate binds Specific shape and chemical environment Catalysis occurs here

6. Enzyme Models Lock and Key model Induced Fit model

7. Mechanism of Enzyme Action Substrate binding Formation of enzyme-substrate complex Catalysis and product release

8. Enzyme Kinetics Michaelis-Menten equation Vmax and Km parameters Graphical representation of kinetics

9. Enzyme Inhibition Competitive inhibition Non-competitive inhibition Uncompetitive inhibition Irreversible inhibition

10. Factors Affecting Enzyme Activity Temperature pH Substrate concentration Enzyme concentration

11. Applications of Enzymes Industrial use (detergents, food processing) Medical use (diagnosis, therapy) Biotechnology and research

12. Examples of Enzymes Amylase (starch → sugar) Protease (protein → amino acids) Lipase (lipids → fatty acids + glycerol)

13. Summary Enzymes are biological catalysts Highly specific and efficient Regulated by multiple factors Important in industry, medicine, and life processes

14. Lock and Key Model Active site has a rigid structure Substrate fits like a key into a lock Explains specificity

15. Induced Fit Model Active site is flexible Substrate binding induces conformational change Explains catalytic efficiency

16. Activation Energy Enzymes lower activation energy barrier Stabilize transition state Speed up reaction rates significantly

17. Competitive Inhibition Inhibitor resembles substrate Competes for active site Can be overcome by increasing substrate concentration

18. Non-Competitive Inhibition Inhibitor binds at allosteric site Reduces enzyme activity regardless of substrate concentration

19. Enzyme Regulation Allosteric regulation Covalent modification (phosphorylation) Feedback inhibition

20. Cofactors and Coenzymes Metal ions (Zn, Mg, Fe) Organic molecules (NAD+, FAD, CoA) Essential for enzyme activity

21. Isoenzymes Different molecular forms of same enzyme Catalyze same reaction Differ in kinetics and regulation

22. Enzyme Applications in Medicine Diagnostic markers (LDH, CK) Therapeutic enzymes (streptokinase) Drug targets