BCH2333A PS 4 2019

Multiple Choice Questions. One correct answer per question. (1 mark each)

1. The protein calcineurin binds to calmodulin with an dissociation rate constant of

8.9x10-5 s-1 and an overall dissociation constant (KD) of 10 nM. The association rate
constant for this binding pair is:

a. 8.9x103 M s-1
b. 8.9x10-11 s-1
c. 8.9x10-3 s-1
d. 8.9x103 M-1 s-1
e. 8.9x105 s-1

2. In a single substrate enzyme-catalyzed reaction, the forward rate constant (formation

of ES) is 2.1x105 M-1s-1, the reverse rate constant (dissociation of ES to E +S) is 9.4x103
s-1, and the catalytic rate constant (turnover of ES to P) is 7.2x102 s-1. From this data, KM
is:

a. 2.23x101 M-1s-1
b. 4.82x10-2 M
c. 2.23x101 M
d. 7.2x102 M
e. 4.82x10-2 M-1

3. Which of the following regarding enzyme catalysis is incorrect?

a. The free energy of the transition state is larger than the free energy of the
intermediates.
b. Enzymes change the overall DG of the reaction.
c. Enzymes work by lowering the energy barrier required to reach the transition
state through transition state stabilization.
d. DDG°‡ is a measure of how much the transition state is being stabilized by the
enzyme.
e. Once the transition state forms, it decays into product at a rate according to the
bond vibrational constant A.

4. The first step in enzyme catalysis is:

a. Restriction of the mobility of substrate

b. Stabilization of the transition state through an increase in non-covalent
interactions
c. Close approximation of substrate and coenzyme
d. Desolvation of active site and substrate
e. Both a and d
Questions 5 to 8 relate to the free energy diagram given below.

5. Considering the free energy diagram, ΔΔG‡ is equal to:

a. A-C
b. B-C
c. C-A
d. B-A
e. C-B

6. What is the correct representation of kcat in the free energy diagram?

a. C
b. B
c. C-B
d. A
e. A-B

7. What is the correct representation of kcat/Km in the free energy diagram?

a. GTSc2-GTSc1
b. GTSc1-GP
c. GTSc2-GS
d. GTSc2-GP
e. B

8. What is the correct representation of k-1/k1 in the free energy diagram?

a. GES-GP
b. GES-GS
c. GP-GS
d. GS-GP
e. GEP-GES
9. The allosteric constant, L, of the enzyme pastase in the presence of substrate alone is
20. When pastase is incubated with substrate and the compound rotinide, L becomes
0.5. However, when incubated with substrate and another compound linguinide, L
becomes 140. Which of the following is true?

a. rotinide is a positive allosteric modulator and linguinide is a negative allosteric

modulator
b. rotinide is a negative allosteric modulator and linguinide is a positive allosteric
modulator
c. rotinide is a positive allosteric modulator and linguinide is a positive allosteric
modulator
d. rotinide is a negative allosteric modulator and linguinide is a negative allosteric
modulator
e. rotinide is a positive allosteric modulator and linguinide is a substrate

For questions 10 and 11, refer to the following Cleland Plot:

S1 S2 P1 P2

E E-S1 E-S1-S2 E-P1-P2 E-P2 E

10. The bisubstrate enzyme-catalyzed reaction shown is:

a. Sequential Random
b. Ping-Pong
c. Allosteric
d. Sequential Ordered
e. Sequential Ternary

11. For this type of enzyme-catalyzed reaction, the following changes would be expected
on a Lineweaver-Burke plot if [S1] was held constant and [S2] was varied:

a. The slope would decrease

b. The slope would increase
c. The x-intercept would increase
d. The y-intercept would increase
e. Both x and y-intercepts would increase but the slope would be unchanged
Short Answer:

12. In the space below, draw the T-A-T base pairing (whole nucleotides) found in
H-DNA. Indicate all H-bonds with dotted lines and circle H-bond donors. Indicate
the major groove and minor groove, and for the adenosine indicate the sugar
edge, Watson-Crick edge, and Hoogsteen edge. (16 marks)
13. What is the ratio of [S] to KM when the velocity of an enzyme-catalyzed reaction is
80% of Vmax?

14. suppose the data shown below are obtained for an enzyme-catalyzed reaction.

[S] (mM) v (mmol mL-1 min-1)

0.1 3.33
0.2 5.00
0.5 7.14
0.8 8.00
1.0 8.33
2.0 9.09
(a) From a double-reciprocal plot, determine KM and Vmax
(b) Assuming that the enzyme present in the system had a concentration of 10-6 M,
calculate its turnover number