1. Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they take place. Lecture 15

2. Lecture 15 – Thursday 2/24/2011 Enzymes Michealis-Menten Kinetics Lineweaver-Burk Plot Enzyme Inhibition Competitive Uncompetitive 2

3. 3

4. 4 1.In the PSSH, we set the rate of formation of the active intermediates equal to zero. If the active intermediate A* is involved in m different reactions, we set it to: 2. The azomethane (AZO) decomposition mechanism is By applying the PSSH to AZO*, we show the rate law, which exhibits first-order dependence with respect to AZO at high AZO concentrations and second- order dependence with respect to AZO at low AZO concentrations.

5. Michaelis-Menten Kinetics. Enzymes are protein like substances with catalytic properties. Enzyme unease. [From Biochemistry, 3/E by Stryer, copywrited 1988 by Lubert Stryer. Used with permission of W.H. Freeman and Company.] 5

6. It provides a pathway for the substrate to proceed at a faster rate. The substrate, S, reacts to form a product P. A given enzyme can only catalyze only one reaction. Example, Urea is decomposed by the enzyme urease. Slow SP Fast 6

7. 7

8. 8

9. A given enzyme can only catalyze only one reaction. Urea is decomposed by the enzyme urease, as shown below. 9 The corresponding mechanism is:

10. 10

11. 11

12. V max =k cat E t Turnover Number: k cat Number of substrate molecules (moles) converted to product in a given time (s) on a single enzyme molecule (molecules/molecule/time) For the reaction 40,000,000 molecules of H 2 O 2 converted to product per second on a single enzyme molecule. 12 H 2 O 2 + E → H 2 O + O + E k cat

13. (Michaelis-Menten plot) V max -r s S 1/2 Solving: K M =S 1/2 therefore K M is the concentration at which the rate is half the maximum rate CSCS Michaelis-Menten Equation 13

14. Inverting yields Lineweaver-Burk Plot slope = K M /V max 1/V max 1/S 1/-r S 14

15. 15

16. 16

17. 17

18. 18

19. 19

20. From before (no competition): Intercept does not change, slope increases as inhibitor concentration increases No Inhibition Competitive Increasing C I 20 Competitive

21. 21

22. Inhibition only has affinity for enzyme-substrate complex Developing the rate law (1) (2) 22

23. Adding (1) and (2) From (2) 23

24. Total enzyme 24

25. Slope remains the same but intercept changes as inhibitor concentration is increased Lineweaver-Burk Plot for uncompetitive inhibition 25

26. 26

27. Both slope and intercept changes Increasing I No Inhibition E + S E·S P + E (inactive)I.E + S I.E.S (inactive) +I -I 27

28. 28

29. 29