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.
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Chapter1: Biochemistry: An Evolving Science
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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.
Transcribed Image Text: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)
Transcribed Image Text: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)
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