BG1131 Molecular Cell Biology for Biomedical Engineers

Homework 2

1. 11-3. What is the relationship between the rate of an enzyme-catalyzed reaction and the rate of
the corresponding uncatalyzed reaction? Do enzymes enhance the rates of slow uncatalyzed
reactions as much as they enhance the rates of fast uncatalyzed reactions?

2. 11-6. Draw a transition state diagram of (a) nonenzymatic reaction and the corresponding
enzyme-catalyzed reaction in which (b) S binds loosely to the enzyme and (c) S binds very tightly
to the enzyme. Compare G‡ for each case. Why is tight binding of S not advantageous?

3. 11-20. Tofu is prepared in such a way as to remove the trypsin inhibitor present in soybeans.
Explain the reason(s) for this treatment.

4. 11-21. Why is the broad substrate specificity of chymotrypsin advantageous in vivo? Why should
this be a disadvantage for some other proteases?

5. 12-5. For an enzymatic reaction, draw curves that show the appropriate relationships between
the variables in each plot: (a) [ES] vs. t, (b) [P] vs. t, (c) vo vs. [E]T

6. 12-11. Calculate KM and Vmax from the following data:

[S] (µM) vo (mM.s-1)

0.1 0.34
0.2 0.53
0.4 0.74
0.8 0.91
1.6 1.04

7. 12-13. Enzyme A catalyzes the reaction SP and has a KM of 50 µM and a Vmax of 100 nM.s-1.
Enzyme B catalyzes the reaction SQ and has a KM of 5 mM and a Vmax of 120 nM.s-1. When 100
µM of S is added to a mixture containing equivalent amounts of enzyme A and B, after one
minute which reaction product will be more abundant: P or Q?

8. 12-19. Determine the type of inhibition of an enzymatic reaction from the following data
collected in the presence and absence of the inhibitor.

[S] (mM) vo (mM.min-1) Vo with I

present
(mM.min-1)
1 1.3 0.8
2 2.0 1.2
4 2.8 1.7
8 3.6 2.2
12 4.0 2.4

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BG1131 Molecular Cell Biology for Biomedical Engineers