ENZYMES

1. ENZYMES

2. Outline • Review – What is an enzyme? • Models of enzyme activity • Lock and key • Induced fit model • Factors affecting enzyme activity • Temperature • pH • Regulation of enzyme activity • Inhibition • Allosterically • Feedback inhibition

3. What is an enzyme? “Biological catalysts”: Speed up reactions in the body

4. Type of protein • Polymer of amino acids • Often globular (spherical) in shape • Contain “active sites” – depressions or grooves on the surface where molecules can bind

5. Binding to an enzyme is very selective: • Active sites interact with specific molecules to catalyze specific reactions • The molecule that binds to an enzyme is called its “substrate”

6. Enzymes lower the activation energy required for a reaction to occur. • Stabilizes the transition state by stretching the bonds of the substrate

7. Some enzymes need to bind to additional molecules to function: • Cofactors (usu. metal ions), or • Coenzymes (act like shuttles btw. enzymes) Apoenzyme – The enzyme, without its cofactors/coenzymes Holoenzyme – The active form, bound to cofactors/coenzymes

8. MODELS OF ENZYME ACTIVITY • Lock and Key model • Induced fit model

9. The “Lock and Key” model • The enzyme has an active site that is unchanging • Substrates bind  chemical process occurs

10. Induced fit model The enzyme can change its shape • One substrate molecule binds weakly • The enzyme’s active site changes shape so that a second substrate molecule can bind • The second substrate binds  Chemical process (rx) occurs

12. FACTORS AFFECTING ENZYME ACTIVITY • Temperature • pH

13. Temperature

14. Increase in activity with temperature (molecules have more energy)... but only to a certain point. • Too much heat will disrupt the 2° , 3° and 4° structure • Denaturation & loss of function

16. Every enzyme has a temperature at which it functions best – this is the optimal temperature • For human enzymes it is usually 37°C (body temp.)

18. pH Enzymes also have optimal pHs • These will vary according to the location in which they function

20. REGULATION OF ENZYME ACTIVITY • Inhibition • Allosterically • Feedback inhibition

21. Competitive inhibition • Are very similar in shape to an enzyme’s substrate. • Bind to the active site, and physicallyblock the correct substrate from binding.

22. Competitive Inhibition

23. Enzyme Efficiency / Rate of Rx

24. Noncompetitive inhibition May be allosteric OR The inhibitor directly affects the enzyme so that it cannot carry out its function. (chemicals that alter the enzyme’s shape and therefore function)

25. Noncompetitive inhibition

26. Noncompetitive inhibition

27. Comparing the 2 inhibitions

28. Allosteric Regulation • Allostericsite – Site on an enzyme that can bind with an effector. • NOT the same as active site. • Effector: • Activator, or • Inhibitor

29. Inhibition vs ActivationInhibitors vs Activators • Some substances can inhibit enzyme function – Inhibitors • Some substances can enhance enzyme function – activators • Inhibition can be either competitiveor noncompetitive

30. Allosteric inhibitor Stabilize the inactive form Allosteric activator Stabilize the active-form See pg. 73, Figure 7

31. Feedback inhibition Often biological reactions occur in a series. Feedback inhibition: The product of a series of enzyme-catalyzed reactions acts to allosterically inhibit an enzyme that acts earlier in the series.

32. WHY IS FEEDBACK INHIBITION important? • 5 minutes discussions: • WHY DO CELLS NEED FEEDBACK? • WHY DO YOU NEED FEEDBACK? • “TWO-WAY” WORLD • ANYONE?

33. SOME APPLICATIONS • Cheese-making • Cow enzyme rennet

34. Insulin for Type 1 diabetics

35. Lactase to digest lactose

36. Homework Pg. 77 #1-8