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[answered] BCH4053 Study Guide EXAM 4 IRSC Koch Please complete this s


Can anyone help me please with this study guide for Biochemistry I.!?



BCH4053 Study Guide EXAM 4 IRSC Koch Please complete this study guide. You may use it (and only it) on your Exam 4.

 

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4.

 

5. Explain the four characteristics of enzymes.

 

Explain and be able to use the classification system for enzymes.

 

Explain how enzymes are specific for their substrates (stereospecific and geometric specificity)

 

Describe the different types of cofactors

 

Explain transition state theory and draw a transition state diagram for a non-catalyzed and an

 

enzyme catalyzed reaction (including multi-step reactions).

 

6. Describe the five types of catalytic mechanisms, recognize them in a reaction mechanism, and

 

draw examples of each type.

 

7. Know the mechanism of RNase A.

 

8. Which residues can act as nucleophiles? Why these residues and not other residues?

 

9. Describe the different ways metalloenzymes use metals to catalyze the reaction.

 

10. Give examples of proximity and orientation effects.

 

11. Describe the evidence we have for enzymes catalyzing reactions by preferential stabilization of

 

transition states and how enzymes bind TS better than the substrate or product.

 

12. Draw the lysozyme mechanism and describe the evidence for the steps in the mechanism.

 

13. Describe the types of catalysis occurring at each step.

 

14. Describe and draw the serine protease active site features.

 

15. Draw the serine protease mechanism and recognize what types of catalysis are occurring at each

 

step.

 

16. Describe how serine proteases exhibit divergent and convergent evolution.

 

17. Explain how low barrier hydrogen bonds may play a role in the serine protease mechanism (in the

 

oxyanion hole)

 

18. Explain how serine proteases like trypsin are regulated.

 

19. Explain the difference between 1st order and 2nd order kinetics

 

20. Derive the Michaelis-Menten equation and know all the assumptions involved in the derivation.

 

21. Draw a Michaelis-Menten plot, label Km, Vmax, saturating conditions and unsaturating conditions.

 

22. Know what Km, kcat, and kcat/Km tell you about the catalysis of an enzyme.

 

23. Know what the diffusion controlled limit is and what it means.

 

24. Draw a Lineweaver-Burk plot for enzyme catalysis. Label the slope and the y-intercept. Be able to

 

determine Km and Vmax if given the slope and the y-intercept.

 

25. Why can?t steady-state kinetics unambiguously establish a reaction mechanism? What else must

 

we know?

 

26. Draw the Cleland notation for bisubstrate reactions, including sequential reactions, and ping-pong

 

reactions.

 

27. Describe the different types of inhibition. Write equations for the different types of inhibition.

 

Draw Lineweaver-Burk plots for the different types of inhibition. Know Table 12-2 on page 374.

 

28. Know how to calculate the KI of an inhibitor given the Km and Km-apparent (Sample Calculation

 

12-5 on page 373).

 

29. Explain allosteric control of an enzyme and feedback inhibition.

 

30. Explain how enzymes are controlled by covalent modification (phosphorylation) using glycogen

 

phosphorylase as an example.

 

31. Explain the process of drug design and development in detail.

 

32. Explain how cytochrome P450 is implicated in adverse drug reactions.

 


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