7. You are studying the effects of a new drug on the activity of your favorite enzyme The results of your assays indicate that the drug acts as a noncompetitive inhibito r. Which of the following changes to the Kim and Vmax allowe that deter mination to be made regarding the drugs actions? A. Km decreased Vmax increased B.Km unchanged Vmax decreased C.Km increased Vmax decreased D.Km decreased Vmax unchanged 8. Drugs that inhibit enzymes in an uncompetitive manner will have which of the following effects on the Michaelis Menten equation-deri ved parameters:Vmax and/or Km? A decrease both Vmax and Km B decrease Km but no effect on Vmax C. decrease Vmax but no change on Km D increase Km but no change in Vmax 9. Which of the following relates to allosteric enzymes? A. they are inactive on their substrates in the absence of accessory proteins B. they possess binding sites for regulatory molecules in addition to substrate binding sites C. they can convert multiple different substrates to product D. they can bind more than one substrate simultaneously 10. You are studying the effects of the addition of a potential pharmaceutical compound on the activity of your enzy me of interest You find that the addition of the c ompound results in an increase in the Km of th e reaction but does not affect the Vmax.Which of the following defines the inhibitory action of the compound? A competitive B .noncompetitive C. suicide D.uncompetitive 11 Enzymes are efficient catalysts because they can do which of the following? A. catalyze reactions that otherwise would not occur B decrease the free energy of activation of reactants C. prevent the conversion of product to substrate D. shift the equilibrium of reactions toward more complete conversion to product 12. Which of the following statements about allosteric enzymes is correct? A Allosteric enzymes display Michaelis -Menten kinetics. B .Allosteric enzymes are usually single subunit enzymes. C. Allosteric enzymes display hyperbolic curve D Allosteric enzymes control metabolism.

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7. You are studying the effects of a new drug on the activity of your favorite enzyme The results of your assays indicate that the drug acts as a noncompetitive inhibito r. Which of the following changes to the Kim and Vmax allowe that deter mination to be made regarding the drugs actions? A. Km decreased Vmax increased B.Km unchanged Vmax decreased C.Km increased Vmax decreased D.Km decreased Vmax unchanged 8. Drugs that inhibit enzymes in an uncompetitive manner will have which of the following effects on the Michaelis Menten equation-deri ved parameters:Vmax and/or Km? A decrease both Vmax and Km B decrease Km but no effect on Vmax C. decrease Vmax but no change on Km D increase Km but no change in Vmax 9. Which of the following relates to allosteric enzymes? A. they are inactive on their substrates in the absence of accessory proteins B. they possess binding sites for regulatory molecules in addition to substrate binding sites C. they can convert multiple different substrates to product D. they can bind more than one substrate simultaneously 10. You are studying the effects of the addition of a potential pharmaceutical compound on the activity of your enzy me of interest You find that the addition of the c ompound results in an increase in the Km of th e reaction but does not affect the Vmax.Which of the following defines the inhibitory action of the compound? A competitive B .noncompetitive C. suicide D.uncompetitive 11 Enzymes are efficient catalysts because they can do which of the following? A. catalyze reactions that otherwise would not occur B decrease the free energy of activation of reactants C. prevent the conversion of product to substrate D. shift the equilibrium of reactions toward more complete conversion to product 12. Which of the following statements about allosteric enzymes is correct? A Allosteric enzymes display Michaelis -Menten kinetics. B .Allosteric enzymes are usually single subunit enzymes. C. Allosteric enzymes display hyperbolic curve D Allosteric enzymes control metabolism.

Answer 1

7. B. Km unchanged, Vmax decreasedNoncompetitive inhibitors bind to an enzyme at a site other than the active site, which does not affect the binding of the substrate (Km remains unchanged) but decreases the maximum reaction rate (Vmax).8. A. decrease both Vmax and KmUncompetitive inhibitors bind only to the enzyme-substrate complex, leading to a decrease in both Vmax and Km.9. B. they possess binding sites for regulatory molecules in addition to substrate-binding sitesAllosteric enzymes have additional binding sites for regulatory molecules that modulate their activity.10. A. competitiveA competitive inhibitor increases the Km of the reaction without affecting the Vmax because it competes with the substrate for the active site.11. B. decrease the free energy of activation of reactantsEnzymes lower the activation energy required for a reaction, thereby increasing the reaction rate.12. D. Allosteric enzymes control metabolism.Allosteric enzymes play a key role in regulating metabolic pathways by responding to the levels of various metabolites.

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