AP Lovrien - Enzymes And Energy
- 1.The active site of an enzyme is the region that
- A.
Binds allosteric regulators of the enzyme.
- B.
Is involved in the catalytic reaction of the enzyme.
- C.
Digests the products of the catalytic reaction.
- D.
Is inhibited by the presence of a coenzyme or a cofactor.
- 2.According to the induced fit hypothesis of enzyme catalysis, which of the following is correct?
- A.
Some enzymes change their structure when activators bind to the enzyme.
- B.
A competitive inhibitor can outcompete the substrate for the active site.
- C.
The binding of the substrate changes the shape of th enzyme's active site.
- D.
The active site creates a microenvironment ideal for the reaction.
- 3.A chemical reaction that has a positive increase in G is correctly described as
- A.
Endergonic
- B.
Endothermic
- C.
Enthalpic
- D.
Spontaneous
- E.
Exothermic
- 4.Which of the following is true of enzymes?
- A.
Enzymes that require a cofactor or ion for catalysis speed up more appreciably than if the enzymes act alone.
- B.
Enzyme function is increased if the three-dimensional structure or conformation of an enzyme is altered.
- C.
Enzyme function is independent of physical and chemical environmental factors such as pH and temperature.
- D.
Enzymes increase the rate of chemical reactions by lowering activition energy barriers.
- 5.When glucose monomers are joined together by glycosidic linkages to form a cellulose polymer, the changes in free energy, total energy, and entropy are as follows:
- A.
+ change in G, + change in H, + change in S
- B.
+ change in G, + change in H, - change in S
- C.
- change in G, - change in H, - change in S
- D.
+ change in G, - change in H, - change in S
- E.
- change in G, - change in H, + change in S
- 6.Succinate dehydrogenase catalyzes the conversion of succinate to fumarate. The reaction is inhibited by malonic acid, which resembles succinate but cannot be acted upon by succinate dehydrogenase. Increasing the ratio of succinate to malonic acid reduces the inhibitory effect of malonic acid. Based on this information, which of the following is correct?
- A.
Succinate dehydrogenase is the enzyme, and fumarate is the substrate.
- B.
Succinate dehydrogenase is the enzyme, and malonic acid is the substrate
- C.
Succinate is the substrate, and fumarate is the product.
- D.
Fumarate is the product, and malonic acid is a noncompetitive inhibitor.
- E.
Malonic acid is the product, and fumarate is a competitive inhibitor.
- 7.Succinate dehydrogenase catalyzes the conversion of succinate to fumarate. The reaction is inhibited by malonic acid, which resembles succinate but cannot be acted upon by succinate dehydrogenase. Increasing the ratio of succinate to malonic acid reduces the inhibitory effect of malonic acid. Based on this information, what is the purpose of using malonic acid in this experiment?
- A.
It is a competitive inhibitor
- B.
It blocks the binding of fumarate.
- C.
It is an allosteric inhibitor.
- D.
It is able to bind to succinate.
- E.
It replaces the usual enzyme.
- 8.Which of the following is likely to lead to an increase in the concentration of ATP in a cell?
- A.
An increase in a cell's anabolic activity.
- B.
An increase in a cell's catabolic activity.
- C.
An increased influx of cofactor molecules.
- D.
An increased amino acid concentration.
- E.
The cell's inceased transport of materials to the environment.
- 9.Which of the following is true for anabolic pathways?
- A.
They do not depend on enzymes.
- B.
They are usually highly spontaneous chemical reactions.
- C.
They consume energy to build up polymers from monomers.
- D.
They release energy as they degrade polymers to monomers.
- 10.Whenever energy is transformed, there is always an increase in the
- A.
Free energy of the system.
- B.
Free energy of the universe.
- C.
Entropy of the system.
- D.
Entropy of the universe.
- E.
Enthalpy of the universe.
- 11.Which of the following types of reactions would decrease the entropy within a cell?
- A.
Dehydration reactions
- B.
Hydrolysis
- C.
Respiration
- D.
Digestion
- E.
Catabolism
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