BCH 361 Final Exam Study Questions

1. Lactic acid fermentation and alcoholic fermentation are oxidation-reduction reactions. What
are the ultimate electron donors and acceptors in these processes? What would happen to a
cell using one of these fermentation processes if the process was inhibited?
2. Although both hexokinase and phosphofructokinase catalyze irreversible steps in glycolysis and
the hexokinase comes first, phosphofructokinase is the rate determining step of glycolysis.
What does this information suggest about the fate(s) of the G6P formed by hexokinase?
3. Why cant the reactions of glycolysis simply be run in reverse to synthesize glucose?
4. Why is it in the muscles best interest to export lactic acid into the blood during intense
exercise? Why is conversion of lactate into glucose in the liver important for the organism?
5. In the liver, fructose can be converted into GAP and DHAP without passing through the
phosphofructokinase-regulated reaction. Show the reactions that make this conversion
possible. Why might ingesting high levels of fructose have deleterious physiological effects?
6. The recommended daily allowance for the vitamin niacin is 15 mg per day. How would
glycolysis be affected by niacin deficiency?

7. Suppose that a microorganism that was an obligate anaerobe suffered from a mutation that
resulted in the loss of triose phosphate isomerase deficiency. How would this loss affect the
ATP yield of fermentation? Could such an organism survive?
8. What is the equilibrium ratio of phosphoenolpyruvate to pyruvate under standard conditions
when [ATP]/[ADP] = 10?
9. What would a Mg+2 deficiency affect glycolysis?
10. The 5-carbon sugar xylose has the same structure as glucose except that it has a hydrogen atom
at C-5 instead of a hydroxymethyl group. When xylose is added to a solution of ATP in the
presence of hexokinase, the rate of ATP hydrolysis increases, yet xylose is not phosphorylated.
Explain.
11. For the hydrolysis of FBP to F6P, G has been found to be -16.7 kJ/mol. ATP hydrolysis has a
G value of -30.5 kJ/mol. Determine the standard free energy change for phosphorylation of
F6P by ATP. What is the equilibrium constant for this reaction? If the cellular concentrations of
[ATP] and [ADP] are maintained constant at 4 mM and 1.6 mM, respectively, what will be the
ratio of [FBP]/[F6P] when the phosphofructokinase reaction reaches equilibrium?
12. The enzyme aldose reductase catalyzes reactions such as the one shown here. Epalrestat is
used as inhibitor of this enzyme to prevent cataract formation. Suggest the manner in which
this inhibition occurs (how and where does the inhibitor interact with the enzyme?).

13. How and why is the regulation of glycolysis and gluconeogenesis coordinated?
14. In terms of carbohydrate metabolism, the liver is primarily a gluconeogenic tissue, while muscles
are glycolytic tissues. Why does this division of labour make sense physiologically?
15. Glycogen is not as reduced as fatty acids are and consequently not as energy rich. Why do
animals store any energy as glycogen? Why not convert all excess fuel into fatty acids?
16. -Amylose is an unbranched polymer of glucose. Why is this polymer not as effective a storage
form of glucose as glycogen?
17. Phosphoglucomutase has a phosphorylated active site residue. The phosphoryl group is slowly
lost by hydrolysis. What is the purpose of this phosphorylated residue? How can this
phosphoryl group be restored?
18. Water is excluded from the active site of glycogen phosphorylase. Predict the effect of a
mutation that allows water to enter the active site.
19. Glycogen debranching enzyme and the transferase activity are found on the same polypeptide.
What advantages are there to having these activities on a single molecule?
20. There must be a way to shut down glycogen degradation once the energy needs have been met
to prevent the wasteful depletion of glycogen. What mechanisms are used to slow down and
stop further glycogen breakdown?
21. Thiamine thiazolone pyrophosphate binds to pyruvate dehydrogenase about 2 x 104 times more
strongly than thiamine pyrophosphate, and is a competitive inhibitor of this enzyme. Why?
22. Shock often causes people to experience oxygen deficiency, which leads to lactic acidosis. Why
would a lack of O2 result in accumulation of lactic acid? One treatment is to administer
dichloroacetate, which inhibits the kinase associated with the pyruvate dehydrogenase complex.
What is the biochemical rationale for this treatment?

23. The American ambassador to Italy in the 1950s became ill when she was staying at the
ambassadorial residence in Rome. The paint on the dining room ceiling, an arsenic-based paint,
was flaking; the wallpaper in her bedroom derived its mellow green colour from cupric arsenite.
Suggest a possible cause of the ambassadors illness.
24. The citric acid cycle is part of aerobic respiration, but no O2 is required for this cycle. Explain this
paradox.
25. The oxidation of malate by NAD+ to form oxaloacetate is highly endergonic under standard
conditions (G = 29 kJ/mol). However, the reaction proceeds readily under physiological
conditions. A) Why? B) Assuming an [NAD+]/[NADH] ratio of 8 and a pH of 7, what is the lowest
[malate]/[oxaloacetate] ratio at which this reaction can proceed?
26. Malonate is a competitive inhibitor of succinate dehydrogenase. How will the concentrations of
citric acid cycle intermediates change immediately after the addition of malonate? Why is
malonate not a substrate for succinate dehydrogenase?

27. Before any oxidation can occur in the citric acid cycle, citrate must be isomerized to isocitrate.
Why?
28. Fatty acid degradation generates a large amount of acetyl-CoA. What is the effect of the
degradation of fatty acids on the pyruvate dehydrogenase complex activity? On glycolysis?
29. Explain how a symmetric molecule (eg. citrate) can react with an enzyme in an asymmetric
manner.
30. Amytal is a barbiturate sedative that inhibits electron flow through Complex I. How would the
addition of amytal to actively respiring mitochondria affect the redox states of the components
of the electron transport chain and the citric acid cycle?
31. Humans have only about 250 g of ATP at any one time, but require about 83 kg of ATP. How is
this discrepancy between requirements and resources reconciled?
32. What is the mechanistic basis for the observation that the inhibitors of ATP synthase also lead to
an inhibition of the electron transport chain?
33. The immediate administration of sodium nitrite (NaNO2) is a highly effective antidote for
cyanide poisoning. What is the basis for the antidote activity of nitrite? [Hint: nitrite oxidizes
ferrohemoglobin to ferrihemoglobin]
34. An inhibitor is added to actively respiring mitochondria. This addition results in the electron
carriers between NADH and QH2 to become more reduced, while those between cytochrome c
and O2 become more oxidized. Where does this inhibitor act?
35. The rate of oxygen consumption by mitochondria increases when ADP is added and then returns
to its initial value when ADP has been converted to ATP. Why does the rate of O2 consumption
increase?
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