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3. NING LI Department of Biochemistry Microbiology and Molecular Biology The Pennsylvania State University USA

4. Enzyme Mechanisms

6. Two Models for Enzyme-Substrate Interaction

7. Induced Conformational Change in Hexokinase

8. Coenzymes

9. Stereo specificity Conferred by an Enzyme

10. Catalytic Mechanisms  Acid-base catalysis  Covalent catalysis  Metal ion catalysis  Electrostatic catalysis  Proximity and orientation effects  Preferential binding to transition state (transition state stabilization)

11. Acid-Base Catalysis

12. Keto-Enol Tautomerism: Uncatalyzed vs. Acid- or Base-Catalyzed

13. Covalent Catalysis: Nucleophiles and Electrophiles Protonated

14. Example of Covalent Catalysis: Decarboxylation of Acetoacetate Lysine side chain  -amino group on enzyme is nucleophile in attack on substrate. Electrophilic “electron sink”

15. Example of Metal Ion Catalysis: Carbonic Anhydrase Carbonic anhydrase catalyzes the reaction: CO 2 + H 2 O HCO 3 − + H +

16. Enolase Mechanism

17. Entropic and Enthalpy Factors in Catalysis

18. Proximity and Orientation Effects

19. Enzymes Are Complementary to Transition State

20. Serine Protease Mechanism: Multiple Catalytic Mechanisms at Work

21. Structure of the Serine Protease Chymotrypsin

22. Serine Protease Substrate Specificity and Active-Site Pockets Substrate specificity in serine proteases through active- site binding of side chain of amino acid residue adjacent to amide bond that will be cleaved. Trypsin cleaves amide bond immediately C- terminal to basic amino acid residues. Chymotrypsin cleaves amide bond immediately C-terminal to hydrophobic amino acid residues.

23. Serine Nucleophile in Serine Proteases

24. Transition State in Proline Racemase Reaction and Transition State Analogs Proline racemase preferentially binds transition state, stabilizing it, and is potently inhibited by transition state analogs.

25. RNA-Based Catalysts (Ribozymes)

26. Cleavage of a Typical Pre-tRNA by Ribonuclease P Ribonuclease P is a ribonucleoprotein (RNA- and protein-containing complex), and the catalytic component is RNA. An even more complex example of an RNA- and protein- containing enzyme system is the ribosome. The central catalytic activity of the ribosome (peptide bond formation) is catalyzed by an RNA component. tRNA substrate of ribonuclease P

27. Catalysis by the Intervening Sequence in Tetrahymena Preribosomal RNA RNA by itself without any protein can be catalytic.

28. Enzyme Regulation

30. Effect of Cooperative Substrate Binding on Enzyme Kinetics Cooperative enzymes do not obey simple Michaelis-Menten kinetics.

31. Regulation of ATCase by ATP and CTP ATP is a positive heterotropic allosteric effector of ATCase, while CTP is a negative heterotropic allosteric effector.

32. Detailed Structure of One Catalytic Subunit and Adjacent Regulatory Subunit of ATCase

33. Quaternary Structure of ATCase in T State and R State

34. X-Ray Structure of Aspartate Transcarbamoylase

35. References: http://www.tutorvista.com/content/biology/biology-iii/cellular- macromolecules/enzymes-classification.php http://www.princeton.edu/~achaney/tmve/wiki100k/docs/Coenzy me.html http://www.cliffsnotes.com/sciences/biology/biochemistry- i/enzymes/chemical-mechanisms-of-enzyme-catalysis

36. Journal of Bioanalysis and Biomedicine Related journals Journal of Bioequivalence & Bioavailability Journal of Chromatography & Separation Techniques Journal of Analytical & Bio analytical Techniques

37. 5th World Congress on Bioavailability and Bioequivalence 3rd International Conference and Exhibition on Bio waivers and Biosimilars Journal of Bioanalysis and Biomedicine Related Conferences

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