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Questions and Answers
Which type of inhibitor competes with the substrate molecules for the active site?
Which type of inhibitor competes with the substrate molecules for the active site?
- Non-competitive inhibitor
- Competitive inhibitor (correct)
- Uncompetitive inhibitor
- Reversible inhibitor
What is the effect of increasing substrate concentration on competitive inhibition?
What is the effect of increasing substrate concentration on competitive inhibition?
- Has no effect on the inhibition
- Reduces Vmax but not Km
- Decreases the affinity of the enzyme for the substrate
- Completely abolishes the inhibition (correct)
Which type of inhibitor does not have any structural resemblance to the substrate?
Which type of inhibitor does not have any structural resemblance to the substrate?
- Reversible inhibitor
- Non-competitive inhibitor (correct)
- Uncompetitive inhibitor
- Competitive inhibitor
In non-competitive inhibition, what happens to the Km value when the substrate concentration is increased?
In non-competitive inhibition, what happens to the Km value when the substrate concentration is increased?
Which type of inhibition reduces both Vmax and Km?
Which type of inhibition reduces both Vmax and Km?
What is the main characteristic of non-competitive inhibitors?
What is the main characteristic of non-competitive inhibitors?
Which inhibitor binds to the enzyme-substrate complex but not to the free enzyme?
Which inhibitor binds to the enzyme-substrate complex but not to the free enzyme?
What is the effect of increasing substrate concentration on uncompetitive inhibition?
What is the effect of increasing substrate concentration on uncompetitive inhibition?
In which type of inhibition does increasing substrate concentration decrease the percentage of enzyme molecules attached to the inhibitor?
In which type of inhibition does increasing substrate concentration decrease the percentage of enzyme molecules attached to the inhibitor?
What is the main characteristic of reversible inhibitors?
What is the main characteristic of reversible inhibitors?
Which of the following is NOT a factor that can make reaction pathways faster?
Which of the following is NOT a factor that can make reaction pathways faster?
Alcohol dehydrogenases (ADH) are classified as which type of enzyme?
Alcohol dehydrogenases (ADH) are classified as which type of enzyme?
What part of an enzyme facilitates the chemical reaction?
What part of an enzyme facilitates the chemical reaction?
Which group of co-enzymes participates in reactions catalyzed by oxidoreductases by donating or accepting hydrogen atoms or electrons?
Which group of co-enzymes participates in reactions catalyzed by oxidoreductases by donating or accepting hydrogen atoms or electrons?
What is the primary focus of enzymology?
What is the primary focus of enzymology?
What class of enzymes catalyze oxidation-reduction reactions, with the substrate being the hydrogen donor?
What class of enzymes catalyze oxidation-reduction reactions, with the substrate being the hydrogen donor?
Which class of enzymes cleave bonds without adding water?
Which class of enzymes cleave bonds without adding water?
Which of the following is a true characteristic of enzymes?
Which of the following is a true characteristic of enzymes?
What percentage of weight do enzymes contain as nitrogen?
What percentage of weight do enzymes contain as nitrogen?
What is the main function of transferase enzymes?
What is the main function of transferase enzymes?
What is the role of enzymes in chemical reactions?
What is the role of enzymes in chemical reactions?
What do metalloenzymes contain that is directly bound to the protein or its non-protein components?
What do metalloenzymes contain that is directly bound to the protein or its non-protein components?
Why is enzyme catalysis considered rapid?
Why is enzyme catalysis considered rapid?
Enzymes are specific to their substrates. What determines substrate specificity?
Enzymes are specific to their substrates. What determines substrate specificity?
What type of reaction do hydrolases catalyze?
What type of reaction do hydrolases catalyze?
What is required for chemical reactions to start?
What is required for chemical reactions to start?
How are proteins hydrolyzed inside the body?
How are proteins hydrolyzed inside the body?
What is the state called when molecules have an initial input of energy during a chemical reaction?
What is the state called when molecules have an initial input of energy during a chemical reaction?
"Almost all enzymes are" what type of biomolecules?
"Almost all enzymes are" what type of biomolecules?
In the Lock and Key Hypothesis, how is the fit between the substrate and the enzyme's active site described?
In the Lock and Key Hypothesis, how is the fit between the substrate and the enzyme's active site described?
What happens in the Induced Fit Hypothesis when a substrate binds to the enzyme?
What happens in the Induced Fit Hypothesis when a substrate binds to the enzyme?
What is denoted by the Km value in enzymology?
What is denoted by the Km value in enzymology?
How does enzyme concentration influence enzymatic reaction velocity?
How does enzyme concentration influence enzymatic reaction velocity?
What can extreme pH levels do to enzymes?
What can extreme pH levels do to enzymes?
How do inhibitors affect enzymic reactions?
How do inhibitors affect enzymic reactions?
At what point does the reaction velocity reach a saturation point in relation to substrate concentration?
At what point does the reaction velocity reach a saturation point in relation to substrate concentration?
What is the impact of temperature on enzyme activity?
What is the impact of temperature on enzyme activity?
What type of reactions do decarboxylases, aldolases, and dehydratases catalyze?
What type of reactions do decarboxylases, aldolases, and dehydratases catalyze?
Which hypothesis suggests that an enzyme changes its shape when a substrate binds?
Which hypothesis suggests that an enzyme changes its shape when a substrate binds?
Flashcards
Competitive Inhibitor
Competitive Inhibitor
Competes with the substrate for the enzyme's active site.
Effect of Substrate on Competitive Inhibition
Effect of Substrate on Competitive Inhibition
Increasing substrate concentration completely reverses the effects of competitive inhibition.
Non-Competitive Inhibitor
Non-Competitive Inhibitor
Does not resemble the substrate's structure and binds elsewhere on the enzyme.
Km Value in Non-Competitive Inhibition
Km Value in Non-Competitive Inhibition
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Uncompetitive Inhibition
Uncompetitive Inhibition
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Irreversible Inhibitors
Irreversible Inhibitors
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Uncompetitive Inhibitor Binding
Uncompetitive Inhibitor Binding
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Effect of Substrate on Uncompetitive Inhibition
Effect of Substrate on Uncompetitive Inhibition
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Substrate Effect on Competitive Inhibition
Substrate Effect on Competitive Inhibition
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Enzymes' Role
Enzymes' Role
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Transferase Enzymes
Transferase Enzymes
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Oxidoreductases (Class 1)
Oxidoreductases (Class 1)
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Lyases (Class 4)
Lyases (Class 4)
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Enzyme Reaction Facilitator
Enzyme Reaction Facilitator
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Co-enzymes for Oxidoreductases
Co-enzymes for Oxidoreductases
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Enzymology Focus
Enzymology Focus
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Metalloenzymes Content
Metalloenzymes Content
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Enzyme Catalysis Speed
Enzyme Catalysis Speed
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Substrate Specificity
Substrate Specificity
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Hydrolases Reaction
Hydrolases Reaction
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Requirements for Reaction Start
Requirements for Reaction Start
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Protein Hydrolysis in Body
Protein Hydrolysis in Body
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Initial Energy Input State
Initial Energy Input State
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Enzyme Biomolecule Type
Enzyme Biomolecule Type
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Lock and Key Hypothesis Fit
Lock and Key Hypothesis Fit
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Induced Fit Hypothesis
Induced Fit Hypothesis
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Km Value
Km Value
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Enzyme Concentration Influence
Enzyme Concentration Influence
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Extreme pH Effects
Extreme pH Effects
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Inhibitors Effect
Inhibitors Effect
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Study Notes
- Enzymes are biological catalysts that facilitate biochemical reactions, catalyzing the formation of isomers (Class 5 isomerases), the joining of two molecules with ATP hydrolysis (Class 6 ligases), or breaking and forming bonds without water or gases (decarboxylases, aldolases, dehydratases).
- The Lock and Key Hypothesis suggests that the fit between the substrate and the enzyme's active site is exact, creating a temporary enzyme-substrate complex.
- In the Induced Fit Hypothesis, the enzyme changes its shape (conformation) when a substrate binds, adapting its active site to the specific substrate and reducing the reaction's activation energy.
- Enzyme reactions are influenced by substrate concentration, enzyme concentration, product concentration, pH, temperature, and inhibitors/activators.
- In enzymic reactions, the reaction velocity increases proportionally with the substrate concentration, reaching a saturation point.
- The enzyme's affinity for the substrate is denoted by the Km value, which is the substrate concentration at half-maximal velocity.
- Enzyme concentration influences the reaction velocity, making it a useful parameter for enzyme assays.
- In a reversible reaction, product concentration affects reaction velocity and can even cause the reaction to reverse or stop when equilibrium is reached.
- Enzymes' activities can be influenced by extreme pH levels, which can denature the enzyme and distort the active site, making it difficult for the substrate to bind.
- Enzyme activity can be affected by temperature, which has an optimum for most enzymes, and denaturation is a concern for some, affecting the enzyme's ability to function.
- Inhibitors can reduce the rate of enzymic reactions by binding to the active site and can be reversible or irreversible.
- Enzymes play crucial roles in many biological pathways, and their functioning can be affected by various factors, including substrate concentration, pH, temperature, and inhibitors/activators.
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