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Free Energy and Enzymes

Quiz by Missy Brewer

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23 questions
Show answers
  • Q1
    Which of the following is an exergonic reaction?
    hydrolysis of glycogen to release glucose monomers
    a dehydration reaction between two monosaccharides to produce a disaccharide
    synthesis of ATP from ADP and Pi
    formation of a peptide bond
    30s
  • Q2
    Which of the following types of reactions would decrease the entropy within a cell
    digestion reactions
    dehydration synthesis reactions that build polymers
    diffusion
    hydrolysis reactions that produce monomers from polymers
    30s
  • Q3
    Which of the following is true for all exergonic reactions?
    Question Image
    The reaction goes only in a forward direction: all reactants will be converted to products, but no products will be converted to reactants.
    A net input of energy from the surroundings is required for the reaction to proceed.
    The products have more total energy than the reactants.
    The reaction proceeds with a net release of free energy.
    30s
  • Q4
    A chemical reaction that has a positive ΔG is best described as
    Question Image
    exergonic
    spontaneous
    in equilibrium
    endergonic
    30s
  • Q5
    For the hydrolysis of ATP to ADP + Pi, the free-energy change is -7.3 kcal/mol under standard conditions. In the cellular environment, however, the free-energy change is about -13 kcal/mol. What can we conclude about the free-energy change for the formation of ATP from ADP and Pi under cellular conditions?
    It is about +26 kcal/mol.
    It is about +13 kcal/mol.
    It is +7.3 kcal/mol.
    It is less than +7.3 kcal/mol.
    60s
  • Q6
    When chemical work is done by an organism, what happens to the heat generated?
    It is used to synthesize ADP.
    It is used to power yet more cellular work.
    It is released to the environment.
    It is used to store energy in the form of ATP.
    30s
  • Q7
    Which of the following statements about enzyme-catalyzed reactions is true?
    Energy from ATP is required to activate the enzyme before it can catalyze the reaction.
    Enzymes always drive reactions toward chemical equilibrium.
    The free-energy change of the reaction is greater than when the same reaction occurs in the absence of an enzyme.
    The rate of the reaction is greater than when the same reaction occurs in the absence of an enzyme.
    45s
  • Q8
    In most exergonic reactions, the reactants capable of interacting to form products typically must first overcome a thermodynamic barrier known as the
    activation energy of the reaction.
    entropy of the reaction
    chemical equilibrium of the reaction
    energy conservation of the reaction
    45s
  • Q9
    A solution of starch at room temperature does not readily decompose to form a solution of simple sugars because
    starch hydrolysis is nonspontaneous
    the hydrolysis of starch to sugar is endergonic
    the starch solution has less free energy than the sugar solution
    the activation energy barrier for this reaction cannot easily be surmounted at room temperature.
    45s
  • Q10
    Which of the following statements regarding enzymes is true?
    Enzymes change the equilibrium point of the reactions they catalyze
    Enzymes increase the rate of a reaction by lowering the activation energy barrier.
    Enzymes increase the rate of a reaction by reducing the rate of reverse reactions.
    Enzymes increase the rate of a reaction by making the reaction more exergonic.
    45s
  • Q11
    The ∆G for a particular enzyme-catalyzed reaction is -20 kcal/mol. If the amount of enzyme in the reaction is doubled, what will be the ∆G for the new reaction?
    -40 kcal/mol
    -20 kcal/mol
    0 kcal/mol
    +20 kcal/mol
    45s
  • Q12
    The ∆G for a particular enzyme-catalyzed reaction is -20 kcal/mol. If the enzyme is removed, what will be the ∆G for the noncatalyzed reaction?
    0 kcal/mol
    -20 kcal/mol
    +20 kcal/mol
    -40 kcal/mol
    45s
  • Q13
    The active site of an enzyme is the region that
    binds substrates for the enzyme.
    is inhibited by the presence of a coenzyme or a cofactor.
    binds allosteric regulators of the enzyme.
    binds noncompetitive inhibitors of the enzyme.
    45s
  • Q14
    The induced fit model of enzyme activity suggests which of the following?
    The binding of an activator alter the conformation of the active site to bind products more tightly.
    The binding of substrate changes the conformation of the active site to bind substrate more tightly.
    The binding of substrate depends on the conformation of the active site.
    The binding of a competitive inhibitor changes the shape of the active site to bind substrate less tightly.
    45s
  • Q15
    A mutation that results in a single amino acid substitution in the active site of an enzyme
    may alter the ∆G for the reaction catalyzed by the enzyme.
    may alter the ability of a noncompetitive inhibitor to bind to the enzyme.
    may alter the ability of an allosteric regulator to alter enzyme activity.
    may change the substrate specificity of the enzyme.
    45s

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