1. ENZYMES IB Topic 3.6 page 74

2. What is an Enzyme? An enzyme is a catalytic PROTEIN – It is effective in small amounts – It is unchanged by the reaction So it’s reusable – It speeds up the rate of reaching equilibrium in a reversible reaction – The shape is very specific – It cannot force a reaction

3. The enzyme active site The starting substance is called the substrate – The substrate is converted to the product The enzyme works by binding to the substrate – The binding point is called the active site – The active site is located on the enzyme As the enzyme and substrate bind, the substrate is raised to a transition state (E A )... – Bonds break – Reactants  Products

4. Enzymes influence the rate of reactions Reactants will form products at a faster rate than without an enzyme – In other words, enzymes speed up the rate of reactions Enzymes lower the energy level needed to start the reaction – Activation energy – Thus, enzymes lower the activation energy

5. Enzymes lower the activation energy of exothermic reactions

6. Lock and Key Hypothesis Due to its precise shape and distinctive chemical properties, each enzyme is specific for a certain substrate or a VERY small group of substrate molecules.

7. Induced Fit Hypothesis Some enzymes change shape when combined with a substrate The active site is then molded into a precise conformation The bonds of the substrate are stretched to make the reaction easier (less energy needed)

8. Enzyme changes shape after it connects with the substrate.

9. Three factors that affect the rate of enzyme-catalyzed reactions 1. Temperature —As temperature increases, molecules are moving faster and are more likely to collide and react. Different enzymes have different optimum temperatures (ex: bacteria in hot springs, plants of the tundra, enzymes in our bodies)

10. 2. Substrate Concentration Increasing the amount of substrate will speed up the rate of reaction. However, there comes a point when there is more substrate than enzyme so adding more substrate molecules will no longer increase the rate of reaction

11. 3. pH — each enzyme has a range of PH in which it functions efficiently

12. Denaturation Denaturation is a structural change in a protein that alters its 3-D shape and causes the loss of its biological properties Denaturation is sometimes permanent and sometimes only temporary

13. Denaturation may be caused by changes in temperature and pH Heat—exposure to heat causes atoms to vibrate violently and this disrupts bonds within globular proteins, and causes changes in the chemical characteristics—usually the change is irreversible (ex: raw vs. cooked egg white) pH—small changes in pH also alter the shape of proteins. However the structure MAY re-form when optimum pH is restored

14. Homework #18-21 page 78

15. Industrial uses of enzymes

16. Lactose-Free Milk The enzyme lactase helps digest lactose in milk Many adults do not produce lactase, so drinking milk causes diarrhea and/or gas Lactose-free milk can be produced using lactase – Whole-cell preparations may not be appropriate for food – Adding and removing enzymes to each product is expensive

17. So immobilized enzymes are used to make the milk

18. Methods of immobilizing enzymes

19. Metabolism consists of chains (linear sequences) and cycles of enzyme- catalzyed reactions

20. Metabolism=anabolic reactions + catabolic reactions Anabolic reactions—larger molecules built from smaller molecules (ex: protein synthesis)—ENERGY REQUIRING/ ENDOTHERMIC Catabolic reactions—larger molecules are broken down (ex: digestion)—ENERGY RELEASING/ EXOTHERMIC

21. Enzymes lower the activation energy of exothermic reactions

22. Competitive Inhibition Example: Carbon dioxide should combine with Rubisco during photosynthesis but can be competitively inhibited by oxygen

23. Non-competitive Inhibition Example: Nerve gas, Sarin blocks acetyl cholinesterase in synapse transmission

24. Allosteric Enzymes Allosteric enzymes have 2 sites. – Active site of the enzyme – Additional site where another substance can lock in – When the other substance is locked in, the active site is non-functional

25. End Product Inhibition—a specific type of Allosteric Inhibition As the end product accumulate, the steps in the product are stopped