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CHM 232Practice Exam 2

1. Which of the following is not required to make holomyoglobin?

a) Fe+2
b) heme
V max
c) 2,3 BPG
K cat
ET
d) apomyoglobin

V max [ S ]
Km [ S ]

Matching. Use the description of each protein listed below to determine which class it belongs to (see list).
2. Aldolasean enzyme that participates in glycolysis in the cytoplasm

a.

structural/fibrous protein

3. Fibronectina protein that holds cells together to make organ tissue

b.

globular/water soluble

4. adrenergic receptora receptor that transmits signals from the

blood to the cytoplasm of cardiac cells. It has mostly non-polar
residues on its outside surface

c.

transmembrane

5. Immunoglobulina protein in your blood that binds to foreign molecules to neutralize them

6. No matter where it is in the body, hemoglobin will always have four of these bound:
a) Fe+2
b) CO2
c) O2
d) 2,3 BPG
7. Enzymes make reactions go faster
a) by eliminating the need to go through the transition state
b) destabilizing the transition state
c) creating an environment which makes the transition state energetically easier to form
d) stabilizing the product by complementing its structure
8. How many chiral carbons does the sugar at right have?
a) 0
b) 1
c) 2
d) 3
e) 4

OH
O
HO
H

H
OH
OH

The following questions refer to the oxygen saturation curve shown at right. This plot shows curves for normal
Hb and Mb (solid lines) and a mutant Hb called Hb Legano (dashed line).
9. Hb Legano binds O2
a) Weaker than normal Hb
b) Cooperatively
c) Tighter than Mb
d) Tighter in the muscles than in the lungs
10. When Hb Legano has 3 O2 bound, how many O2 are bound
to normal Hb?
a) 0
b) 1
c) 2
d) 3
e) 4
11. The mutation in Hb Legano likely causes the change in the saturation curve (compared to normal Hb) by
a) Shifting Hb Legano more to the relaxed state
b) Preventing heme from binding to Hb Legano
c) Causing Hb Legano to fall apart into monomers
d) The same effect seen with the binding of 2,3 BPG
12. What is the P50 of Hb Legano?
a) ~ 50%
b) ~ 76%
c) ~ 28 torr
d) ~ 75 torr
13. Compared to someone with normal Hb, a patient with Hb Legano will have trouble
a) Binding enough O2 in the lungs
b) Binding more than 1 O2 at a time
c) Getting full saturation of Mb
d) Dumping enough O2 in the muscles
14. Once aspirin binds to its target enzyme and forms a covalent bond, the enzyme cannot be used again. As an
inhibitor, aspirin is therefore:
a) competitive
b) irreversible
c) non-competitive
d) uncompetitive

15. Which of the following is a similarity between cellulose and glycogen?

a) They are both polymers of glucose
b) They are both branched polymers
c) They are molecules that plants use to store energy
d) They both contain (14) glycosidic linkages
16. Tagatose is the C-4 epimer of fructose. Which of the following is L-tagatose? (a-e, left to right)

HO

OH

OH

OH

OH

OH

HO

OH

HO

OH

OH

OH

OH

OH

HO

HO

OH

HO

HO

HO

HO

OH

OH

OH

OH

17. Which of the following represents the correct attack for the formation of a cyclic monosaccharide?
(a-d, left to right)
H

OH

HO

O
C

HO

HO

HO

HO

OH

HO

OH

OH

O
OH

OH

OH

OH

OH
H

OH

18. Why cant myoglobin bind O2 cooperatively?

a) It is permanently locked in the tense state
b) Its heme has a Fe+3 instead of Fe+2
c) It can only bind one O2 at a time
d) Its quartenary structure is 22 instead of 22
19. Refer to the chart at right to determine which answer is true:
a) Enzyme A carries out its chemical catalysis faster than Enzyme B
b) Enzyme B carries out its chemical catalysis faster than Enzyme A
c) Enzyme A and Enzyme B carry out their chemical catalysis
the same rate
vmax
d) It is not possible to determine which enzyme carries out its
KM
chemical catalysis faster from the data shown
Amount of
enzyme

at
Enzyme A
200 mol/s
12 mM
4 mol

Enzyme B
250 mol/s
2 mM
5 mol

The following questions refer to the disaccharide shown at right:

20. The linkage is
a) (15)
b) (24)
c) (16)
d) (15)
e) (24)
f) (16)
g) The same as the linkage found in cellulose

OH
O

HO

O
OH

HO
O

OH

OH
HO
HO

21. The two sugars are

a) an aldose (left) and ketose (right)
b) both aldoses
c) a ketose (left) and aldose (right)
d) both ketoses
22. If you switched the chirality of carbon #3 of the left sugar, you would get
a) D-glucose
b) L-glucose
c) D-mannose
d) L-mannose
23. Which of the sugars in the disaccharide can mutorotate?
a) The left sugar can mutorotate, but the right sugar cannot
b) The right sugar can mutorotate, but the left sugar cannot
c) Both can mutorotate
d) Neither can mutorotate
24. This sugar
a) Is a reducing sugar because its right monosaccharide can linearize to form a free aldehyde
b) Is a reducing sugar because its left monosaccharide can linearize to form a free aldehyde
c) Is not a reducing sugar because neither of its monosaccharides can linearize to form a free aldehyde
d) Is not a reducing sugar because it only contains alcohols, not free aldehydes
25. When vo is 75% of vmax, what is the relationship between [S] and Km
a) [S] = Km
b) [S] > Km
c) [S] < Km
d) Cannot be determined from information given

26. Give the name of the each of the following modified sugars. Make sure you include D/L and / in the
name.
O
-

HO

HO

O
O
OH

OH
OH

____________________________

27.

OH

OH

OH

HO

____________________________

OH

NH3

OH

__________________________

Plants use L-galactose to make vitamin C. Draw the structure of -L-galactose:

27. Our cells have an enzyme that changes ribulose 5-phosphate

(shown at right in the enzyme active site) into ribose-5phosphate. Based on the structure of the substrate shown
and what you know about ribose, what type of isomerization
is that reaction? ______________________________

OH
O
OH
H

b. The reaction gets going when an aspartate residue acts as a

base to remove a proton from carbon #1. In general this
type of residue is called a________________________

OH

H
O

O
P

O
-

c. In the hypothetical active site below, put in three

appropriate residues (side-chain only) that would help bind
ribulose-5-phosphate. You should use three different
residues, and three different types of interactions.

d.

The Michaelis-Menten plots for ribulose-5-phosphate is shown below. Give the following kinetic
constants from the graph:
KM: _______________vmax: ________________
60

e. This enzymes can also use ribulose as a substrate

(instead of ribulose-5-phosphate). Ribulose binds
more weakly to the enzyme than ribulose-5phosphate, but the chemical reaction takes place just
as fast after it is bound. On the graph, carefully draw
the Michaelis-Menten curve that you would expect for
ribulose as a substrate (assuming you use the same
amount of the enzyme).

Vo [mol/s]

50
40
30
20
10
0
0

10

20

30

40

[ribulose-5-phosphate] mM

f. Transform your values from part d. above and show how

this ribulose-5-phosphate data would look on a
Lineweaver Burke graph (use a solid line).

0.1
0.09
0.08
0.07

1/[Vo] (s/mol)

g. Ribitol-5-phosphate (shown at right) is an

inhibitor of this enzyme. Given that it
looks so similar to ribulose-5-phosphate
(the normal substrate), use a dashed line to
draw what you would expect to see for a
Lineweaver Burke plot in the presence of
this inhibitor.

0.06

OH

0.05
0.04
0.03
0.02

OH

0.01

OH
OH
O

O
P

-2
O

-1

0
1/[S] (1/mM)