BIO Test 2
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| When chemical, transport, or mechanical work is done by an organism, what happens to the heat generated? | It is lost to the environment
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| Which of the following characteristics is most likely to be associated with an enzyme that catalyzes two different chemical reactions? | Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures.
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| Which of the following is a primary function of the active site of an enzyme? | It catalyzes the reaction associated with the enzyme.
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| A series of enzymes catalyze the reactions in the metabolic pathway X → Y → Z → A. Product A binds to the enzyme that converts X to Y at a position remote from its active site. This binding decreases the activity of the enzyme. A functions as | an allosteric inhibitor
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| Which of the following statements is true of metabolism in its entirety in all organisms? | Metabolism consists of all the energy transformation reactions in an organism.
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| Which of the following statements describes a key component of the induced fit hypothesis of enzyme catalysis? | Binding of substrate to the active site changes the shape of the active site of an enzyme.
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| Which of the following statements describes a common characteristic of catabolic pathways? | They are exergonic and provide energy that can be used to produce ATP from ADP and i.
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| When ATP releases some energy, it also releases inorganic phosphate. What happens to the inorganic phosphate in the cell? | It may be used to form a phosphorylated intermediate.
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| Which of the following statements about enzyme function is true? | Enzymes increase the rate of chemical reactions by lowering activation energy barriers.
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| How might a change of one amino acid at a site, distant from the active site of an enzyme, alter the substrate specificity of an enzyme? | by changing the three-dimensional conformation of the enzyme
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| Which of the following statements describes a central role that ATP plays in cellular metabolism? | ATP provides energy coupling between exergonic and endergonic reactions.
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| How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction? | By binding to an allosteric site, thus changing the shape of the active site of the enzyme
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| Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as | A cofactor necessary for enzyme activity
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| Which of the following statements is true for a system at chemical equilibrium? | The system can do no work.
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| Which of the following types of reactions would decrease the entropy within a cell? | Anabolic reactions
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| Which of the following terms most precisely describes the cellular process of breaking down large molecules into smaller ones? | catabolism (catabolic pathways)
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| Which of the following statements describes the first law of thermodynamics? | Energy cannot be created or destroyed.
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| HIV is the virus that causes AIDS. In the mid-1990s, researchers discovered an enzyme in HIV called protease. Once the enzyme's structure was known, researchers began looking for drugs that would fit into the active site and block it. | competitive inhibition
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| The relationship between catabolism and anabolism is most similar to the relationship between which of the following pairs of terms | exergonic; endergonic
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| In a metabolic pathway, succinate dehydrogenase catalyzes the conversion of succinate to fumarate. The reaction is inhibited by malonic acid, a substance that resembles succinate but cannot be acted upon by succinate dehydrogenase. | Succinate is the substrate, and fumarate is the product in the reaction
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