Practice Exam for Midterm

Lkklkkkkkkkkkkl;

1. Fill in the following table about the amino acids Serine and Cysteine in the
dipeptide shown above.
Property Serine Cysteine
Classification

Level(s) of protein structure

the side chain can potentially
be involved in.
Present in TPI? (Yes/No)

Present in Chymotrypsin
(Yes/No)

2. Circle the amino acid side chain (R group) that could receive a phosphate group
from a protein kinase.

3. What are the three amino acids that can be phosphorylated?

 Practice Exam for Midterm

4. For a chemical reaction where the equilibrium constant (Keq) is much greater than
one.
a. What sign is the ΔG’o

b. Is this reaction endergonic?

c. Is the reverse reaction favorable? Is it at all possible for this reaction to go in

reverse?

d. How would a catalyst affect the equilibrium constant for the reaction?

5. How do exergonic reactions actually power endergonic reactions in the body? Use
the example of Glutamine biosynthesis in your response.
 Practice Exam for Midterm

6. Chymotrypsin is a very well studied proteolytic enzyme. Answer the following

questions about Chymotrypsin.

a. What features of the Chymotrypsin active site account for its specificity?

b. What features of the enzyme active site account for its catalytic ability? Describe
the general sequence for proteolysis of a peptide.

7. Answer the following questions about the Glycolysis metabolic pathway.

a. Which steps of Glycolysis required NAD+ as a substrate?

b. Which steps of Glycolysis are significantly exergonic and irreversible?

c. What is the key regulated step in Glycolysis?

d. During which step(s) of Glycolysis does ADP accept a phosphate group from a
high energy carbon-phosphate intermediate?

8. ATP Synthase catalyzes the reversible reaction Enz-(ATP) <->Enz-(ADP

-1
+
Pi).Given that the rate constant for the forward reaction is 10 s and that of the reverse
is 24s-1. Calculate the Keq. Does this number surprise you, considering the standard
free energy change for the hydrolysis of ATP at 298 K?

9. You find an unknown compound labeled “Chemical X.” To determine the identity
of the compound, you test it with a sample of enzyme and take kinetic data before and
after the addition of the unknown compound. What class of compound is Chemical
X?
 Practice Exam for Midterm

10. Identify which statements are false.

a. Enzymes speed up a reaction by increasing the rate of the forward rate constant but
not the reverse rate constant.
b. A competitive inhibitor will increase the KM of an enzyme for a substrate, and will
decrease the Vmax.
c. Enzymes speed up a reaction by decreasing the enthalpy and entropy of activation.
d. The equilibrium constant for a reaction can be expressed as a product of the rate
constants for the forward and reverse reactions.
e. A reaction can be first order in one direction and second order in the opposite
direction.
f. Enzymes can’t change the Keq of a reaction, but they can increase both the forward
and reverse rate constants.
g. For a first order reaction in which the k-1 >> k1, you would expect, at equilibrium, for the ratio
of products/reactants >> 1.

11. Lactate fermentation occurs in humans when oxygen is unavailable.

a. What is its purpose?

b. What other type of fermentation do anaerobic organisms undergo?

c. The reaction is drawn below. Name/Draw the Letters

 Practice Exam for Midterm

12. There are 6 classes of enzymes:

I. Oxidoreducatases
II. Transferases
III. Hydrolases
IV. Lyases
V. Isomerases
VI. Ligases

a. What class is chymotrypsin? (hint: think of the reaction mechanism)

b. Hexokinase

c. Triose Phosphate Isomerase

d. Monoamine oxidase

e. Aldolase
.
f. Alcohol Dehydrogenase

h. Trypsin

i. Proteases

13. ‘Feedback inhibition,’ is an example of which of the following:

a. homotropic allosteric activation b. homotropic allosteric repression

c. heterotropic allosteric activation d. heterotropic allosteric repression

14. When substrate binding activates the enzyme, this is an example of:

a. homotropic allosteric activation b. homotropic allosteric repression

c. heterotropic allosteric activation d. heterotropic allosteric repression

15. A sigmoid, or ‘S’ shaped Michaelis-Menten plot of V0 vs. [S], is typically seen
with which of the following:

a. homotropic allosteric activation b. homotropic allosteric repression

c. heterotropic allosteric activation d. heterotropic allosteric repression

 Practice Exam for Midterm

Please answer the following regarding Michaelis-Menton enzyme kinetics:

16. Label the above graph with: the axes, Vmax, ½ Vmax and indicate which Vo position is
equivalent to KM (do your best to arbitrarily position these labels).

17. What are the assumptions used to derive the graph above?

18. Write the general equation that best describes the Michaelis-Menten graph:

19. Draw a Lineweaver Burke plot for an enzyme in the presence and absence of an irreversible
inhibitor.

Written by Alex Vu, Tony Yu, Ben Lewin, Mandi Ma, Dr. Aaron
Coleman and Sam Rana during Summer Session II 2011