Explore key concepts of enzyme catalysis with questions on active sites, Michaelis-Menten kinetics, competitive inhibition, and allosteric control. This quiz enhances understanding of enzyme behavior and reaction dynamics, essential for students and professionals in biochemistry.
Competitive inhibition can be overcome by the addition of large amounts of substrate to a reaction.
The addition of large amounts of substrate to a reaction cannot overcome the effect of a competitive inhibitor.
A competitive inhibitor can bind to the enzyme-substrate complex.
The Vmax of a reaction decreases in the presence of a competitive inhibitor.
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Allosteric inhibition
Feedback inhibition
Competitive inhibition
Non-competitive inhibition
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Km, the Michaelis constant, is defined as the concentration of substrate required for the reaction to reach maximum velocity.
Km, the Michaelis constant, is defined as the dissociation constant of the enzyme-substrate complex.
Km, the Michaelis constant, is a measure of the affinity the enzyme has for its substrate.
Km, the Michaelis constant, is expressed in terms of the reaction velocity.
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A competitive inhibitor and substrate can bind simultaneously to the enzyme.
The Vmax and Km (Michaelis constant) for a reaction are unchanged in the presence of a competitive inhibitor.
The Km for a reaction remains unchanged in the presence of a competitive inhibitor.
The Vmax for a reaction remains unchanged in the presence of a competitive inhibitor.
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Allosteric enzymes are typically single-subunit enzymes.
Allosteric enzymes show greater sensitivity to changes in substrate concentration compared to classical type enzymes with hyperbolic kinetics.
Allosteric enzymes show Michaelis-Menten kinetics.
Allosteric enzymes show reduced sensitivity to changes in substrate concentration compared to classical type enzymes with hyperbolic kinetics.
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The active site of an enzyme binds the substrate of the reaction it catalyses more tightly than it does the transition state intermediate
The active site of an enzyme binds the substrate of the reaction it catalyses less tightly than it does the transition state intermediate.
The active site of an enzyme binds the product of the reaction it catalyses more tightly than it does the transition state intermediate.
The active site of an enzyme is complementary to the substrate of the reaction it catalyses
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He rate of formation of the transition state intermediate determines the overall free energy change of the reaction.
The active site of an enzyme is perfectly complementary to the substrate in its ground state.
The rate of formation of the transition state intermediate determines the overall reaction rate.
Natural substrates bind to enzymes more tightly than transition state analogues
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DNA gyrase
DNA polymerase
Carbonic unhydrase
Pepsin
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Succinic dehydrogenase by malonic acid
Cytochrome oxidase by cyanide
Hexokinase by glucose-6-phosphate
Carbonic anhydrase by carbon dioxide
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