The inhibitory effect of an uncompetitive inhibitor is greater at high [S] than at low [S]. Explain this observation.
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Q: Define the term minimum inhibitory concentration and their uses.
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Q: Suggest a simple method to determine whether a reaction is being inhibited bu a competitive or…
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Q: Why is the transition-state analog not necessarily the same as a competitive inhibitor
A: Competitive inhibitor is the inhibitor having the similar shape as the substrate of the enzyme and…
Q: Is the inhibitor competitive or uncompetitive or non-competitive and why?
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Q: The inhibitory effect of an uncompetitive inhibitor is greater at high [S] thanat low [S]. Explain…
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Q: Why does the apparent KM decrease in the presence ofan uncompetitive inhibitor?
A: An enzyme inhibitor is a molecule that binds to enzyme and decreases its activity. By binding to the…
Q: A Without inhibitor
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Q: Identify the two forms of mixed inhibition and briefly describe how the two forms differ?
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Q: Minimum inhibitory concentrations
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Q: draw and label a Michaelis-Menten plot showing the effect of a compentitive inhibitor
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Q: What is the difference between pure and mixed noncompetitive inhibition?
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Q: Define “reciprocal inhibition” and explain its importance
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Q: Explain the differences and similarities in the three kinds of reversible inhibition. Include what…
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Q: why is non-competitive inhibiton a special type of mixed inhibiton
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Q: 5.5 Explain the effect of each type of inhibitor on the apparent kinetic parameters:
A:
Q: The nerve gas sarin acts as a poison by covalently bonding to a hydroxyl group in the active site of…
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Q: Chymotrypsin preferentially binds the transition state. What is meant by that?
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Q: What TYPE of inhibition is observed in the following: S E S
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Q: Inhibition of oxamic acid causes what type of inhibition?
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at low [S]. Explain this observation.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F3c36674e-3e5a-40fc-95de-e6a1a68d321e%2Fc325338d-d6f8-41a1-ba26-87b25ef5812a%2Fbaevtnl_processed.png&w=3840&q=75)
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- The inhibitory effect of an uncompetitive inhibitor is greater at high [S] thanat low [S]. Explain this observation.What is the minimum inhibitory concentration indicated in the following image?Using equilibrium argument, why does Km apparently increase, decrease or stay the same in uncompetitive inhibition?
- If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?why is non-competitive inhibiton a special type of mixed inhibiton?
- Is the inhibitor competitive or uncompetitive or non-competitive and why?The nerve gas sarin acts as a poison by covalently bonding to a hydroxyl group in the active site of the enzyme acetylcholinesterase. This binding results in a higher-than-normal amount of acetylcholine at a nerve synapse, resulting in muscle spasms. From this description, would you expect sarin to be a competitive, noncompetitive, or irreversible inhibitor? noncompetitive inhibitor irreversible inhibitor competitive inhibitorGive an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.
- If the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible?Write a balanced equation for the hydrolysis of cGMP, catalyzed by cGMP phosphodiesterase. Would you expect an inhibitor of this enzyme to potentiate or antagonize the action of Viagra? Explain.Chymotrypsin preferentially binds the transition state. What is meant by that?