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Which of the following statements regarding enzyme inhibition is correct?
- a)Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor protein.
- b)Competitive inhibitors often bind to the enzyme irreversibly.
- c)Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzymes.
- d)Non-competitive inhibition of an enzyme can be overcome by adding large amount of substrate.
Correct answer is option 'C'. Can you explain this answer?
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Which of the following statements regarding enzyme inhibition is corr...
Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzymes. Most competitive inhibitors function by binding reversibly to the active site of the enzyme. As a result, many sources state that this is the defining feature of competitive inhibitors.
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Which of the following statements regarding enzyme inhibition is corr...
Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzymes.
Explanation:
Enzymes are proteins that catalyze biochemical reactions in living organisms. Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. There are different types of enzyme inhibition, including competitive inhibition, non-competitive inhibition, and uncompetitive inhibition.
Competitive inhibition occurs when a substrate and an inhibitor molecule both compete for binding to the active site of an enzyme. The active site is the region on the enzyme where the substrate binds and the catalytic reaction takes place. In competitive inhibition, the inhibitor molecule is structurally similar to the substrate and can bind to the active site, preventing the substrate from binding.
Key Points:
- Competitive inhibition occurs when a substrate and an inhibitor molecule both compete for binding to the active site of an enzyme.
- The inhibitor molecule is structurally similar to the substrate and can bind to the active site.
- When the inhibitor is bound to the enzyme, it prevents the substrate from binding and inhibits the catalytic activity of the enzyme.
- Competitive inhibitors do not irreversibly bind to the enzyme. They can be displaced by increasing the concentration of the substrate.
- Competitive inhibition can be overcome by increasing the concentration of the substrate because the substrate outcompetes the inhibitor for binding to the active site.
- The inhibitor is reversible, meaning that it can bind and unbind from the enzyme.
- Competitive inhibitors do not permanently alter the enzyme's structure or function.
- The binding of the competitive inhibitor is usually weaker than the binding of the substrate.
- Competitive inhibition is a common mechanism used by cells to regulate enzyme activity.
- Examples of competitive inhibitors include drugs that target enzymes involved in disease processes, such as antibiotics and anticancer drugs.
In conclusion, option 'C' is the correct statement regarding enzyme inhibition because competitive inhibition occurs when the substrate and the inhibitor compete for the active site on the enzyme.
Explanation:
Enzymes are proteins that catalyze biochemical reactions in living organisms. Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. There are different types of enzyme inhibition, including competitive inhibition, non-competitive inhibition, and uncompetitive inhibition.
Competitive inhibition occurs when a substrate and an inhibitor molecule both compete for binding to the active site of an enzyme. The active site is the region on the enzyme where the substrate binds and the catalytic reaction takes place. In competitive inhibition, the inhibitor molecule is structurally similar to the substrate and can bind to the active site, preventing the substrate from binding.
Key Points:
- Competitive inhibition occurs when a substrate and an inhibitor molecule both compete for binding to the active site of an enzyme.
- The inhibitor molecule is structurally similar to the substrate and can bind to the active site.
- When the inhibitor is bound to the enzyme, it prevents the substrate from binding and inhibits the catalytic activity of the enzyme.
- Competitive inhibitors do not irreversibly bind to the enzyme. They can be displaced by increasing the concentration of the substrate.
- Competitive inhibition can be overcome by increasing the concentration of the substrate because the substrate outcompetes the inhibitor for binding to the active site.
- The inhibitor is reversible, meaning that it can bind and unbind from the enzyme.
- Competitive inhibitors do not permanently alter the enzyme's structure or function.
- The binding of the competitive inhibitor is usually weaker than the binding of the substrate.
- Competitive inhibition is a common mechanism used by cells to regulate enzyme activity.
- Examples of competitive inhibitors include drugs that target enzymes involved in disease processes, such as antibiotics and anticancer drugs.
In conclusion, option 'C' is the correct statement regarding enzyme inhibition because competitive inhibition occurs when the substrate and the inhibitor compete for the active site on the enzyme.
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Which of the following statements regarding enzyme inhibition is correct?a)Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor protein.b)Competitive inhibitors often bind to the enzyme irreversibly.c)Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzymes.d)Non-competitive inhibition of an enzyme can be overcome by adding large amount of substrate.Correct answer is option 'C'. Can you explain this answer?
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