Enzyme Inhibition Rate of reaction Normal enzyme Inhibitor A Inhibitor B Substrate concentration Figure 4: Enzyme inhibition; Source: Wikimedia Commons 20. Describe the effect of each inhibitor on the enzymatic reaction rate. Additionally, predict which inhibitor is competitive and which is noncompetitive; provide your reasoning.
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1.) You are studying the enzyme catalyzed reaction and how it is affected by the competitive inhibitor below. State how this inhibitor will affect each of the kinetic parameters below and briefly explain why. a. KM b. Vmax c. kcat d. Catalytic efficiency 2.) Calculate the dissociation constant (Ki) for the below inhibitor if you used 12 ÎĽM of that inhibitor in the reaction. Express your response in units of ÎĽM. What is the mode of inhibition?
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Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is equal to normal, and as the substrate concentration is increased more and more, the rate of reaction remains the same as the normal rate. What can be concluded about the unknown substance? Select the correct answer below: It is a competitive inhibitor. It is a noncompetitive inhibitor. It is an evenly divided mixture of competitive and noncompetitive inhibitors. It is neither a competitive nor a noncompetitive inhibitor.
In the equation below, substrate $C$ is an allosteric inhibitor to enzyme 1. Which of the following is another mechanism necessarily caused by substrate $C ?$ $$\mathrm{A} \underset{\text { enzyme } 1}{\longrightarrow} \mathrm{B} \underset{\text { enzyme } 2}{\longrightarrow} \mathrm{C}$$ (A) Competitive inhibition (B) Irreversible inhibition (C) Feedback enhancement (D) Negative feedback
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