You performed a kinetic study of the enzyme lipase and you obtained the following double reciprocal (Lineweaver-Burk) plot: 4 3 y = 4.3511x + 1.8889 -0.5 -0.3 -0.1 0.1 0.3 0.5 0.7 0.9 1/[S] When you performed the same kinetic study in the presence of an inhibitor, you obtained a new line that had y-intercept 3 and x-intercept -0.3. Based on this information select all correct statements about this inhibitor. This is mixed inhibitor. When this inhibitor is present apparent Km of enzyme decreases. This inhibitor prevents substrate from binding to the enzyme. This is uncompetitive inhibitor. When this inhibitor is present apparent Vmax of enzyme decreases. When this inhibitor is present apparent Km of enzyme increases. This inhibitor can bind to either enzyme or enzyme-substrate complex. OA/T

You performed a kinetic study of the enzyme lipase and you obtained the following double reciprocal (Lineweaver-Burk) plot: 4 3 y = 4.3511x + 1.8889 -0.5 -0.3 -0.1 0.1 0.3 0.5 0.7 0.9 1/[S] When you performed the same kinetic study in the presence of an inhibitor, you obtained a new line that had y-intercept 3 and x-intercept -0.3. Based on this information select all correct statements about this inhibitor. This is mixed inhibitor. When this inhibitor is present apparent Km of enzyme decreases. This inhibitor prevents substrate from binding to the enzyme. This is uncompetitive inhibitor. When this inhibitor is present apparent Vmax of enzyme decreases. When this inhibitor is present apparent Km of enzyme increases. This inhibitor can bind to either enzyme or enzyme-substrate complex. OA/T

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter30: Capillary Electrophoresis, Electrochromatography, And Field-flow Fractionation

Section: Chapter Questions

Problem 30.9QAP

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