Name: _________________________

Student ID: _____________________

Ryerson University
Department of Chemistry and Biology

Mid-Term Examination
October 2015
BCH 361
Advanced Biochemistry I

Examination Instructions and Information

1.

This examination consists of two parts: A. Short Answer, and B. Multiple Choice.

2.

Answer each short answer question in the space provided. Ink is preferred. Illegible work will not be given
credit.

3.

Use a HB or soft pencil to fill in the bubble on the sheet provided for the Multiple Choice questions. The
answers on the bubble sheet are your official final answers for the multiple choice section. Failure to indicate
your answer will result in a score of 0 for each multiple choice question with no answer on the bubble sheet.

4.

Calculators are allowed. No other aids, including cell phones are allowed. Cell phones, PDAs, and other
electronic equipment should be turned off and placed with your bag or coat at the front of the room; they are
not allowed on your person or at your desk.

5.

You are not permitted to remove any examination materials from the examination room.

-1

-1

R = 8.3145 Jmol K
-23
-1
kB = 1.3807 10 JK
-1
-1
F = 96 485 JV mol
-34
h = 6.6261 10 Js
T = 25C unless otherwise indicated

A. Short Answer

/25

B. Multiple Choice

/25

TOTAL

/50

BCH 361 Midterm

October 2015
SECTION A SHORT ANSWER QUESTIONS
Answer each question in the space provided. If you need additional space, use the back of the page.

1. The following pH-rate profile for an engineered selenocysteine containing peroxidase was published (Yu et al
(2005) J. Biol. Chem. 280, 11930-11935). What information can you obtain from this plot? Is any additional data
required? Provide details and briefly explain your answer.
(5)

2. An enzyme contains a metal ion, Zn+2, in its active site. With reference to the diagram below, what is the most
likely role of the metal ion?
(2)

3. In the study of the inhibition of an enzyme, the following Lineweaver-Burk plot was created with the kinetic
data. What evidence does this plot provide regarding the type of inhibition? How would the inhibition constant
be derived from the data shown in this plot? Show this using a schematic secondary plot. How does this type of
inhibitor cause inhibition of the enzyme on a molecular level?
(5)

Page 1 of 6

4. A pathway is shown below along with the G values for each step. Which step(s) of this pathway would be most
suitable sites for regulation? Why? What would happen if this pathway was not regulated?
(5)

5. The enzyme glycerol kinase catalyzes the phosphorylation of glycerol with ATP. Inhibition studies show that
glycerol-3-phosphate is a competitive inhibitor vs. glycerol and a mixed inhibitor vs. ATP.
(5)
a. What type of binding order is observed? Which, if any, substrate binds first? Briefly explain your
rationale.

b. Show shape and identify the characteristic features of a primary plot of the enzyme kinetics for this type
of BiBi reaction using your choice of a Lineweaver-Burk or Hanes-Wolf plot.

6. The activity of phosphotriesterase on several V-type chemical warfare agents was tested (Bigley et al. (2015)
Biochemistry 54, 5502-5512), as shown in the table below. Which of these is the better substrate for the
enzyme? Explain your rationale briefly.
Electron donor kcat (s-1) KMNAD(P) (mM) kcat/KM (M-1s-1)
DMVX
0.021
1.1
1.9 x 101
DEVR

0.201

0.38

(3)

5.6 x 102

Page 2 of 6