Enzyme

Tutorial

1. What are the general characteristics of enzyme active sites?

2. What is the fundamental mechanism by which enzymes enhance the rate of chemical
reactions?

3. The illustrations below show the reaction-progress curves for two different reactions.
Indicate the activation energy as well as the ∆G for each reaction. Which reaction is
endergonic? Exergonic?

(A) (B) 20. A tenacious mu

binds a substrate 10
zyme. What is the ef
the binding of the t
21. A question of st
Free energy

Substrate Product
coenzyme for the en
enzyme was purified
dium as well as from
Product Substrate pyridoxal phosphat
Reaction progress Reaction progress measured by incub
for the amount of e
14. Mountain climbing. Proteins are thermodynamically ing results were obt

unstable. The $G of the hydrolysis of proteins is quite neg-
100%
ative, yet proteins can be quite stable.
4. What is feedback inhibition? Why is it a useful property? Explain this apparent
paradox. What does it tell you about protein synthesis? Enzyme activity
Tymoczko: Biochemistry: A Short Course, 2E
5. The kinetics of an enzyme are measured as a function of substrate concentration in the
Perm. Fig.: 6009 Suggest
Newwhy Fig.: 06-UN01
15. Protection. the enzyme lysozyme, which
remaining

presence and in the absence of 2 mM inhibitor (I).

First Draft: 2011-07-06
degrades cell walls of some bacteria, is present in tears.
-1
16. Stability matters.Velocity (µmol minute
Transition-state analogs, ) which can be
[S] (µM) used as enzyme inhibitors
No inhibitor Inhibitor
and to generate catalytic antibod-
3
ies, are often difficult to synthesize. Suggest a 4.1
10.4 0%
reason.  2
5 14.5 6.4
10 22.5
17. Match’em. Match the Keq values with the 11.3
appropriate
30 $G° values.  1 33.8 22.6 (a) Why does the a
90 40.5 33.8 the time of incubati
1
Keq $G° (kJ mol ) (b) Why does the am
(a) What are the values of Vmax and K
(a) 1 in the absence of inhibitor? In its presence?
28.53
M cells decline more r
5
(b) 10 11.42
(b) What type of inhibition is it?
(c) 10 4
5.69
2 Challenge Problems
(d) 10 0
(e) 101 22.84 22. Free energy, yet
18. Free energy! Consider the following reaction: tion of 0.1 M gluco
add the enzyme p
Glucose 1-phosphate N glucose 6-phosphate the reaction.  1
6. The kinetics of the enzyme considered in problem 6 are measured in the presence of a
different inhibitor. The concentration of this inhibitor is 100 mM.

Velocity (µmol minute-1)
[S] (µM) No inhibitor Inhibitor
3 10.4 2.1
5 14.5 2.9
10 22.5 4.5
30 33.8 6.8
90 40.5 8.1

(a) What are the values of Vmax and KM in the presence of this inhibitor? Compare them with
those obtained in problem 20.

(b) What type of inhibition is it?

7. For the reaction of glucose with oxygen to produce carbon dioxide and water;

Glucose + 6O2 6CO2 + 6H2O

the ∆G° is -2880 kJ mol-1, a strongly exergonic reaction. However, a sample of glucose can be
maintained indefinitely in an oxygen-containing atmosphere. Reconcile these two
statements.

8. Suggest a reason for carrying out enzymatic reactions in buffer solutions.

9. Distinguish between the lock-and-key and induced-fit models for binding of a substrate to
an enzyme.

10. What features distinguish enzymes that undergo allosteric control from those that obey
the Michaelis–Menten equation?


11. What are some possible advantages to the cell in combining phosphorylation with
allosteric control?