Enzymes - AP Biology
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Which of the following factors has an effect on the rate at which enzymes catalyze a reaction?
Which of the following factors has an effect on the rate at which enzymes catalyze a reaction?
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The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.
The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.
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Consider the reaction:
This reaction is catalyzed by an enzyme called carbonic anhydrase. Which of the following will result from increasing the concentration of carbonic anhydrase?
Consider the reaction:
This reaction is catalyzed by an enzyme called carbonic anhydrase. Which of the following will result from increasing the concentration of carbonic anhydrase?
Tap to reveal answer
Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.
The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.
Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.
The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.
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In non-physiological reactions an increase in temperature will increase the reaction rate; however, in physiological reactions there is an optimum temperature at which an enzyme operates. Increasing the temperature beyond this will not increase enzyme activity or reaction rate. What explains this phenomenon?
In non-physiological reactions an increase in temperature will increase the reaction rate; however, in physiological reactions there is an optimum temperature at which an enzyme operates. Increasing the temperature beyond this will not increase enzyme activity or reaction rate. What explains this phenomenon?
Tap to reveal answer
There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.
You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.
There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.
You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.
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Which of the following characteristics affects the function of an enzyme?
Which of the following characteristics affects the function of an enzyme?
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Temperature, pH, and substrate concentration all affect the function of an enzyme; therefore, the correct answer is all of these.
Temperature, pH, and substrate concentration all affect the function of an enzyme; therefore, the correct answer is all of these.
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Which of the following statements about enzymes is correct?
Which of the following statements about enzymes is correct?
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The correct answer to this question is they function under a narrow pH range.
Enzymes do indeed function under a narrow pH range. A narrow pH range is needed because enzymes speed up reactions by lowering the activation energy and in order to do this very specific conditions must be met. Coenzymes are not always needed and they are certainly not consumed in a reaction. Enzymes also are proteins so they are polymers of amino acids, not carbohydrates. Also enzymes have no part in the creation of ATP.
The correct answer to this question is they function under a narrow pH range.
Enzymes do indeed function under a narrow pH range. A narrow pH range is needed because enzymes speed up reactions by lowering the activation energy and in order to do this very specific conditions must be met. Coenzymes are not always needed and they are certainly not consumed in a reaction. Enzymes also are proteins so they are polymers of amino acids, not carbohydrates. Also enzymes have no part in the creation of ATP.
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Which model of enzyme substrate binding posits that there is a transition state that develops before the reactants undergo change
Which model of enzyme substrate binding posits that there is a transition state that develops before the reactants undergo change
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The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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The induced fit model better explains enzyme substrate binding than does the lock and key model. The induced fit model explains which of the following, that is not explained by the lock and key model
The induced fit model better explains enzyme substrate binding than does the lock and key model. The induced fit model explains which of the following, that is not explained by the lock and key model
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model accounts for the broad specificity of enzymes as the active site is not rigid, but can undergo a conformational change to better fit the substrate binding.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model accounts for the broad specificity of enzymes as the active site is not rigid, but can undergo a conformational change to better fit the substrate binding.
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This model of enzyme and substrate interaction posits that the active site of the enzyme undergoes conformational change when the correct substrate binds
This model of enzyme and substrate interaction posits that the active site of the enzyme undergoes conformational change when the correct substrate binds
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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The lock and key model of enzyme substrate binding posits that
The lock and key model of enzyme substrate binding posits that
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The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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Which is NOT true of the lock and key model of enzyme substrate bonding?
Which is NOT true of the lock and key model of enzyme substrate bonding?
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The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model does not account for a transition state during which the shape of the active site changes to better fit the substrate.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model does not account for a transition state during which the shape of the active site changes to better fit the substrate.
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How do enzymes speed up a reaction?
How do enzymes speed up a reaction?
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Enzymes speed up reactions through lowering the activation energy, of the energy needed to break bonds of reactants. The activation energy is lowered through stabilizing the transition state; the active site of the enzyme better fits the substrate, allowing bonds to more readily be broken, requiring less energy.
Enzymes speed up reactions through lowering the activation energy, of the energy needed to break bonds of reactants. The activation energy is lowered through stabilizing the transition state; the active site of the enzyme better fits the substrate, allowing bonds to more readily be broken, requiring less energy.
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The induced fit model better explains enzyme substrate binding than does the lock and key model. The induced fit model explains which of the following, that is not explained by the lock and key model
The induced fit model better explains enzyme substrate binding than does the lock and key model. The induced fit model explains which of the following, that is not explained by the lock and key model
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model accounts for the broad specificity of enzymes as the active site is not rigid, but can undergo a conformational change to better fit the substrate binding.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model accounts for the broad specificity of enzymes as the active site is not rigid, but can undergo a conformational change to better fit the substrate binding.
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This model of enzyme and substrate interaction posits that the active site of the enzyme undergoes conformational change when the correct substrate binds
This model of enzyme and substrate interaction posits that the active site of the enzyme undergoes conformational change when the correct substrate binds
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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The lock and key model of enzyme substrate binding posits that
The lock and key model of enzyme substrate binding posits that
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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Which model of enzyme substrate binding posits that there is a transition state that develops before the reactants undergo change
Which model of enzyme substrate binding posits that there is a transition state that develops before the reactants undergo change
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit.
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Which is NOT true of the lock and key model of enzyme substrate bonding?
Which is NOT true of the lock and key model of enzyme substrate bonding?
Tap to reveal answer
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model does not account for a transition state during which the shape of the active site changes to better fit the substrate.
The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced fit model states that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit. The induced fit model does not account for a transition state during which the shape of the active site changes to better fit the substrate.
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How do enzymes speed up a reaction?
How do enzymes speed up a reaction?
Tap to reveal answer
Enzymes speed up reactions through lowering the activation energy, of the energy needed to break bonds of reactants. The activation energy is lowered through stabilizing the transition state; the active site of the enzyme better fits the substrate, allowing bonds to more readily be broken, requiring less energy.
Enzymes speed up reactions through lowering the activation energy, of the energy needed to break bonds of reactants. The activation energy is lowered through stabilizing the transition state; the active site of the enzyme better fits the substrate, allowing bonds to more readily be broken, requiring less energy.
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Which of the following factors has an effect on the rate at which enzymes catalyze a reaction?
Which of the following factors has an effect on the rate at which enzymes catalyze a reaction?
Tap to reveal answer
The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.
The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.
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Consider the reaction:
This reaction is catalyzed by an enzyme called carbonic anhydrase. Which of the following will result from increasing the concentration of carbonic anhydrase?
Consider the reaction:
This reaction is catalyzed by an enzyme called carbonic anhydrase. Which of the following will result from increasing the concentration of carbonic anhydrase?
Tap to reveal answer
Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.
The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.
Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.
The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.
← Didn't Know|Knew It →
In non-physiological reactions an increase in temperature will increase the reaction rate; however, in physiological reactions there is an optimum temperature at which an enzyme operates. Increasing the temperature beyond this will not increase enzyme activity or reaction rate. What explains this phenomenon?
In non-physiological reactions an increase in temperature will increase the reaction rate; however, in physiological reactions there is an optimum temperature at which an enzyme operates. Increasing the temperature beyond this will not increase enzyme activity or reaction rate. What explains this phenomenon?
Tap to reveal answer
There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.
You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.
There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.
You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.
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