A) the resulting enzyme can catalyze the breakdown of lipids for energy.
B) energy is captured in the peptide bonds between the amino acids that compose lipase.
C) synthesis of lipase increases entropy as compared with the free amino acids.
D) an increase in temperature is required to make the enzyme.
E) free amino acids have greater free energy than the lipase enzyme.
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Multiple Choice
A) Aligning the substrate atoms so they are brought into proximity with each other, favoring the chemical reaction
B) Altering the hydrophobicity of a substrate (e.g., making a hydrophobic molecule hydrophilic)
C) Altering the shape of the enzyme to favor expulsion of the product
D) Aligning two different substrates such that their reactive atoms are held as far apart as possible
E) Chemically cleaving the substrate so that the small substrate fragments can enter solution more easily
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Multiple Choice
A) The 3ʹ -OH bond of the ribose sugar
B) The P-O bond of the third phosphate group
C) In the N-C bonds of the adenine base group
D) In hydrogen bonds with another ATP molecule
E) In solution with H2O
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Multiple Choice
A) Competitive inhibitors bind to the active site, whereas noncompetitive inhibitors change the shape of the active site.
B) Competitive inhibitors have a higher energy of activation than noncompetitive inhibitors have.
C) Noncompetitive enzyme inhibitors contain magnesium, whereas competitive inhibitors contain iron.
D) Noncompetitive enzyme inhibitors are reversible, whereas competitive inhibitors are irreversible.
E) They function at different pH values.
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Multiple Choice
A) feedback inhibition.
B) phosphatase activity.
C) reversible phosphorylation.
D) noncovalent regulation.
E) allosteric regulation.
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Short Answer
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Multiple Choice
A) Add more glucose.
B) Add more phosphate.
C) Add a higher concentration of reactant and allow it to make more product.
D) Add ATP as an energy source for the forward reaction (G = ‒7.1 kJ/mol) to make more product.
E) Add an enzyme to lower the ΔG of the reaction so more product is made.
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Short Answer
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Multiple Choice
A) Light electrical mechanical chemical
B) Mechanical electrical chemical light
C) Light chemical electrical mechanical
D) Light mechanical chemical electrical
E) Electrical mechanical light chemical
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Multiple Choice
A) Products > transition state > reactants
B) Reactants > transition state > products
C) Transition state > reactants > products
D) Transition state > products > reactants
E) Reactants > products > transition state
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Multiple Choice
A) add more mevalonate.
B) add more HMG-CoA.
C) lower the temperature of the reaction.
D) add a prosthetic group.
E) lower the rate constant of the reaction.
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Multiple Choice
A) increase.
B) decrease.
C) stay the same.
D) increase, but only with an increase in enzyme amount.
E) decrease, but only with a decrease in enzyme amount.
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Multiple Choice
A) There is 1 kJ of mechanical energy available to do work.
B) The amount of usable energy decreases with each conversion, so less than 1 kJ of energy is available for mechanical work.
C) All of the reactions involved are anabolic, so there is 0.25 kJ of mechanical energy available.
D) All of the reactions involved are exergonic, so the number of kilojoules of mechanical energy produced is greater than the 1 kJ input.
E) All of the reactions involved are endergonic, so without constant input of energy, no mechanical energy is produced.
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Multiple Choice
A) N-ethylmaleimide is a competitive inhibitor of alcohol dehydrogenase.
B) N-ethylmaleimide is a reversible inhibitor of alcohol dehydrogenase.
C) N-ethylmaleimide is an activator of alcohol dehydrogenase.
D) N-ethylmaleimide is a noncompetitive inhibitor of alcohol dehydrogenase.
E) N-ethylmaleimide is an irreversible inhibitor of alcohol dehydrogenase.
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Multiple Choice
A) The blue tracing represents the catalyzed reaction because it has a larger G than the uncatalyzed reaction.
B) The blue tracing represents the catalyzed reaction because it has a larger activation energy than the uncatalyzed reaction.
C) The red tracing represents the catalyzed reaction because it has a smaller G than the uncatalyzed reaction.
D) The red tracing represents the catalyzed reaction because it has a smaller activation energy than the uncatalyzed reaction.
E) The red tracing represents the catalyzed reaction because it leads to the formation of more products than the uncatalyzed reaction.
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Short Answer
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View Answer
Multiple Choice
A) The average person produces about 40 kg of ATP per day.
B) The average person hydrolyzes about 40 kg of ATP per day.
C) ATP is readily hydrolyzed in water.
D) ATP is chemically stable and can be stored easily for extensive periods of time.
E) ATP can be moved around the cell for its optimal use at a different location.
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Multiple Choice
A) ATP, ADP, AMP, adenosine
B) AMP, ADP, ATP, adenosine
C) Adenosine, ATP, AMP, ADP
D) ATP, AMP, ADP, adenosine
E) ADP, adenosine, AMP, ATP
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Multiple Choice
A) Fumarase uses no coenzyme but requires one Fe2+ ion at its active site.
B) Fumarase catalyzes both the forward and reverse reactions between fumarate and malate.
C) Fumarase binds one fumarate molecule and one water molecule the same way for every reaction.
D) The active site of fumarase contains a histidine and a lysine that function as an acid and a base, respectively, during catalysis.
E) Mutation of the active site lysine to other amino acids obliterates or severely reduces activity in fumarase.
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Multiple Choice
A) Total G of the reaction will decrease.
B) The disorder of the system will decrease.
C) The temperature at which the reaction occurs will change.
D) The reaction is anabolic in nature.
E) The reaction is highly complex.
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