When considered in the context of the Michaelis-Menten model of enzyme kinetics, a noncompetitive inhibitor will have what effect? A noncompetitive inhibitor _______ the $K_m$ of an enzyme-catalyzed biochemical reaction. A noncompetitive inhibitor _______ the $V_{max}$ of an enzyme-catalyzed biochemical reaction. increases; does not alter does not alter; increases, does not alter; decreases decreases; does not alter
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This binding does not prevent the substrate from binding to the active site, but it does change the shape of the enzyme, making it less effective at catalyzing the reaction. Show moreā¦
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1.10 Noncompetitive Inhibitor (2 points) As we have discussed, you can analyze the kinetic properties of an enzyme by measuring its velocity of catalysis at various substrate concentrations and plotting [S] vs V, or I[S] vs 1/V. You can also analyze the properties of an enzyme inhibitor by carrying out the same experiment and graphic analysis in the presence of the inhibitor. If you do this for a noncompetitive inhibitor, what differences will you see when you compare the enzyme kinetics to an uninhibited control? Vmax will decrease and KM will increase. Vmax and KM both remain the same with a noncompetitive inhibitor. Vmax and KM will both decrease. Vmax will be unchanged, but KM will increase. (E) Vmax will decrease, but KM will be unchanged.
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When comparing an enzymatic reaction in the presence of a competitive enzyme inhibitor to the uninhibited reaction, the inhibited reaction will have a lower Vmax and unchanged Km; the same Vmax and a higher Km; or a lower Vmax and a lower Km.
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QUESTION 26 A noncompetitive inhibitor of an enzyme-catalyzed reaction a. reduces KM and increases Vmax. b. reduces KM and reduces Vmax. c. increases KM and increases Vmax. d. increases KM and reduces Vmax.
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