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Questions and Answers
What effect does a mixed inhibition have on Vmax and Km?
What effect does a mixed inhibition have on Vmax and Km?
- Vmax and Km both decrease
- Vmax decreases, Km remains relatively unchanged (correct)
- Vmax and Km both increase
- Vmax increases, Km decreases
In irreversible inhibition, how do nerve gases and toxins typically impact enzymes?
In irreversible inhibition, how do nerve gases and toxins typically impact enzymes?
- Change Km or Vmax (correct)
- Decrease Vmax only
- Increase Km only
- Leave Km and Vmax unaffected
In the Lineweaver–Burk double reciprocal plot, where do the lines intersect for mixed inhibition?
In the Lineweaver–Burk double reciprocal plot, where do the lines intersect for mixed inhibition?
- Near the y-axis, to the right of the x-axis
- At the origin (0,0)
- Near the x-axis, to the left of the y-axis (correct)
- Near the x-axis, to the right of the y-axis
What type of inhibition does not compete with the substrate for the active site?
What type of inhibition does not compete with the substrate for the active site?
How is allosteric control defined in enzyme regulation?
How is allosteric control defined in enzyme regulation?
Which mechanism-based inhibitor falls into the irreversible inhibitors category?
Which mechanism-based inhibitor falls into the irreversible inhibitors category?
In the context of enzyme kinetics, what happens when a reversible inhibitor binds to an enzyme?
In the context of enzyme kinetics, what happens when a reversible inhibitor binds to an enzyme?
Which type of reversible inhibitor reacts with the enzyme to form a covalent bond, rendering the protein inactive?
Which type of reversible inhibitor reacts with the enzyme to form a covalent bond, rendering the protein inactive?
How do competitive inhibitors affect the Michaelis-Menten kinetics compared to uninhibited reactions?
How do competitive inhibitors affect the Michaelis-Menten kinetics compared to uninhibited reactions?
Which statement is true regarding the Lineweaver–Burk plot for competitive inhibition?
Which statement is true regarding the Lineweaver–Burk plot for competitive inhibition?
What is the dissociation constant (KI) used to measure in relation to inhibitors?
What is the dissociation constant (KI) used to measure in relation to inhibitors?
How does an irreversible inhibitor differ from a reversible inhibitor in terms of enzyme action?
How does an irreversible inhibitor differ from a reversible inhibitor in terms of enzyme action?
In noncompetitive inhibition, where does the inhibitor bind in relation to the enzyme's active site?
In noncompetitive inhibition, where does the inhibitor bind in relation to the enzyme's active site?
What happens to the KM value in noncompetitive inhibition?
What happens to the KM value in noncompetitive inhibition?
Which type of inhibition involves binding to an enzyme-substrate complex?
Which type of inhibition involves binding to an enzyme-substrate complex?
What is the effect of increasing substrate concentration in noncompetitive inhibition?
What is the effect of increasing substrate concentration in noncompetitive inhibition?
Which plot is commonly used to analyze enzyme kinetics and distinguish between types of inhibition?
Which plot is commonly used to analyze enzyme kinetics and distinguish between types of inhibition?
How does noncompetitive inhibition affect Vmax in enzyme kinetics?
How does noncompetitive inhibition affect Vmax in enzyme kinetics?
Which type of inhibition involves altering the enzyme's structure around the active site?
Which type of inhibition involves altering the enzyme's structure around the active site?
In which type of inhibition does increasing substrate concentration reduce inhibitor binding?
In which type of inhibition does increasing substrate concentration reduce inhibitor binding?
What happens to the slope of a Lineweaver–Burk plot when an inhibitor is present?
What happens to the slope of a Lineweaver–Burk plot when an inhibitor is present?
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Study Notes
Enzyme Inhibition
- Mixed inhibition: affects both Vmax and Km.
- Irreversible inhibition: nerve gases and toxins typically bind covalently to the enzyme, rendering it inactive.
Lineweaver-Burk Plot
- Mixed inhibition: lines intersect at a point other than the y-axis.
- Competitive inhibition: lines intersect at the same point on the y-axis.
- The Lineweaver-Burk plot is used to analyze enzyme kinetics and distinguish between types of inhibition.
Types of Inhibition
- Non-competitive inhibition: does not compete with the substrate for the active site, binds to an allosteric site, and alters the enzyme's structure.
- Allosteric control: regulation of enzyme activity by binding of molecules to sites other than the active site.
- Uncompetitive inhibition: involves binding to an enzyme-substrate complex.
- Reversible inhibition: inhibitor binds to the enzyme, reducing its activity, but can be removed, restoring enzyme activity.
- Irreversible inhibition: inhibitor binds covalently to the enzyme, rendering it inactive.
Enzyme Kinetics
- Competitive inhibition: increases Km, but Vmax remains unchanged.
- Non-competitive inhibition: Km remains unchanged, but Vmax decreases.
- Increasing substrate concentration in non-competitive inhibition: has no effect on inhibitor binding.
- Increasing substrate concentration in competitive inhibition: reduces inhibitor binding.
Inhibitors
- Dissociation constant (KI): measures the binding affinity of an inhibitor to an enzyme.
- Mechanism-based inhibitor: falls into the irreversible inhibitors category, forms a covalent bond with the enzyme, rendering it inactive.
- Covalent inhibitor: reacts with the enzyme to form a covalent bond, rendering the protein inactive.
Enzyme Regulation
- Allosteric control: defined as the regulation of enzyme activity by binding of molecules to sites other than the active site.
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