C483 Final Exam Study Guide
The final will be held in Ballantine 013 at 8-11AM on Friday, July 31. There will be no excused
absences for the final.
There are two parts to the final exam.
A. 100 points covering chapters 17-19. This exam will look much like what you have
seen in the other midterm exams.
B. 100 point cumulative exam. This exam will cover major themes and integrated
concepts for the course. It will be about 1/3 multiple choice, 1/3 short answer, and 1/3 problems
taken directly from the list below. These questions will also serve as a good review for the major
topics of the course. You are encouraged to use them as a study guide. You may work with
others in the class to work through these problems. The instructor and AI will not assist you or
provide answers.
Questions:
1. Pratt question 13.20
2. Pratt question 14.14
3. Pratt question 14.40
4. Given a name, draw chemical structures of: ATP, all amino acids, all glycolysis intermediates,
acetyl CoA, all citric acid cycle intermediates
5. Explain the logic of these pathway regulations:
A. Phosphofructokinase, not hexokinase, is the main regulation site of glycolysis.
B. SuccinylCoA inhibits the entry of acetyl CoA into the citric acid cycle.
C. NADH inhibits pyruvate dehydrogenase.
D. Citrate inhibits the citric acid cycle and activates acetyl-CoA carboxylase.
E. Insulin leads to activation of glycogen synthase.
6. Describe each cycle/transport system (compounds, compartments, tissues) and explain its
purpose:
A. malate/aspartate shuttle
B. citrate transport system
C. Cori cycle
D. glucose/alanine cycle
7. For each of these cofactors, explain its chemical function and give an example of a type of
enzyme that would use it: TPP, PLP, biotin, FAD, NADPH
8. Integrated metabolism
A. A molecule of glucose that you eat can eventually be transformed into part of a fatty acid that
you store. Circle the pathways/cycles below that are part of this overall flow of carbon atoms.
Cross out any that are not.
Gluconeogenesis, beta-oxidation, citric acid cycle, glycolysis, urea cycle, fatty acid synthesis
B. Trace the metabolic path of this glucose molecule through the enzymes it encounters along
the way to being made into fat. Write all the enzymes in the list below into the proper places in
the figure below. If the enzyme is not used, write its name in the “not used” box. If it is used,
write the enzyme in the order that the carbon atoms from glucose encounter the enzymes.
Pyruvate dehydrogenase, fumarase, aldolase, lactate dehydrogenase, pyruvate kinase, acetyl CoA
carboxylase, fatty acid synthase, hexokinase, carnitine acyltransferase, ATP synthase
B. What is the minimum number of glucose molecules that would be necessary to be the carbon source
for synthesis of a 16-carbon fatty acid through this pathway?
C. How many net glucose can be made from one molecule of a 16-carbon fatty acid?
9. Integrated metabolism
A. A molecule of glutamate that you eat can eventually be transformed into part of a glucose
molecule that you store in your liver. Circle the pathways/cycles below that are part of this
overall transformation. Cross out any that are not.
Gluconeogenesis, pentose phosphate pathway, glycogen synthesis, glycolysis, citric acid cycle
B. Trace the metabolic path of this glutamate molecule through the intermediates it becomes on
the way to being glucose. Draw the structure of glutamate and glucose in the boxes. Indicate the
order of transformation by writing “1”, “2”, etc next to each appropriate structure. Cross out the
one molecule not involved in this pathway.
C. The nitrogen atom of glutamate must be removed by oxidative deamination, and is
incorporated into a molecule that is excreted. Draw the structure of this molecule.
10. Drawing figures. In the spaces below, draw an appropriately shaped figure, including
necessary axis labels.
A. A titration curve for lysine, with a side chain pKa of 10.5.
B. A DNA melting curve for a poly(AT) sequence and a poly(GC) sequence (indicate which is
poly(AT) and which is poly(GC))
C. A plot of initial velocity versus substrate concentration for a Michaelis-Menton enzyme.
D. The same plot as (B), but the enzyme is treated with a competitive inhibitor
E. a pH profile for an enzyme with two key ionized residues: a cysteine with pKa 4.2 and a
Histidine with pKa 8.2
F. Saturation curve for myoglobin and hemoglobin (indicate which is which)