Use this graph to draw new curves that reflect enzyme activity for each of the conditions in parts a-c. (Label the curves E + Act, E+ Inh, and E-mut.) Then answer part d. a. The enzyme in the presence of a heterotropic allosteric activator (E + Act). b. The enzyme in the presence of a heterotropic allosteric inhibitor (E + Inh). c. A mutant enzyme (E-mut) in which the predominant structure in solution consists of monomers that have a higher affinity for the substrate than that of the tetrameric enzyme. d. Show on the plot how to determine the Km of E-mut. 28. The following graph shows the activity of an enzyme that functions as a homotetramer in which substrate concentration is plotted versus vo/Vmax (ratio of the initial velocity relative to the maximum velocity). Vo хешл 1 0.8 0.6 0.4 0.2 0 [Substrate] (mM)
Use this graph to draw new curves that reflect enzyme activity for each of the conditions in parts a-c. (Label the curves E + Act, E+ Inh, and E-mut.) Then answer part d. a. The enzyme in the presence of a heterotropic allosteric activator (E + Act). b. The enzyme in the presence of a heterotropic allosteric inhibitor (E + Inh). c. A mutant enzyme (E-mut) in which the predominant structure in solution consists of monomers that have a higher affinity for the substrate than that of the tetrameric enzyme. d. Show on the plot how to determine the Km of E-mut. 28. The following graph shows the activity of an enzyme that functions as a homotetramer in which substrate concentration is plotted versus vo/Vmax (ratio of the initial velocity relative to the maximum velocity). Vo хешл 1 0.8 0.6 0.4 0.2 0 [Substrate] (mM)
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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