I Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate S binds reversibly to enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and regenerate the free enzyme E. E+S ES →E+ P For many enzymes, the rate of the reaction increases with substrate concentration, till it reaches a plateau, Vmax because the enzyme is sàturated, or all enzyme molecules are bound to substrate molecules. This is shown below in the graph as curve A. The substrate concentration that gives you a rate that is halfway to Vmax is called the Km, and is a useful measure of how quickly reaction rate increases with substrate concentration. a. Which of the curves B or C Vmax best demonstrates enzyme B. activity in the presence of a competitive inhibitor? Explain briefly why. 1/2 Vmax Vmax -- C b. Which of the curves B or C best demonstrates enzyme 1/2 Vmax- activity in the presence of a noncompetitive inhibitor? Explain briefly why. Km Km Substrate concentration [S] Do you observe a change in Vmax and Km in presence of competitive or noncompetitive inhibitor from the graph. Yes/No. Explain briefly why or why not с. Initial rate of reaction (v)

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I Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate S
binds reversibly to enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to
generate a product P and regenerate the free enzyme E.
E+S ES →E+ P
For many enzymes, the rate of the reaction increases with substrate concentration, till it reaches a plateau, Vmax
because the enzyme is sàturated, or all enzyme molecules are bound to substrate molecules. This is shown below
in the graph as curve A. The substrate concentration that gives you a rate that is halfway to Vmax is called the Km,
and is a useful measure of how quickly reaction rate increases with substrate concentration.
a.
Which of the curves B or C
Vmax
best demonstrates enzyme
B.
activity in the presence of a
competitive inhibitor? Explain
briefly why.
1/2 Vmax
Vmax --
C
b.
Which of the curves B or C
best demonstrates enzyme
1/2 Vmax
activity in the presence of a
noncompetitive inhibitor? Explain
briefly why.
Km
Km
Substrate concentration [S]
Do you observe a change in Vmax and Km in presence of competitive or noncompetitive
inhibitor from the graph. Yes/No. Explain briefly why or why not
C.
Initial rate of reaction (v)
Transcribed Image Text:I Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate S binds reversibly to enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and regenerate the free enzyme E. E+S ES →E+ P For many enzymes, the rate of the reaction increases with substrate concentration, till it reaches a plateau, Vmax because the enzyme is sàturated, or all enzyme molecules are bound to substrate molecules. This is shown below in the graph as curve A. The substrate concentration that gives you a rate that is halfway to Vmax is called the Km, and is a useful measure of how quickly reaction rate increases with substrate concentration. a. Which of the curves B or C Vmax best demonstrates enzyme B. activity in the presence of a competitive inhibitor? Explain briefly why. 1/2 Vmax Vmax -- C b. Which of the curves B or C best demonstrates enzyme 1/2 Vmax activity in the presence of a noncompetitive inhibitor? Explain briefly why. Km Km Substrate concentration [S] Do you observe a change in Vmax and Km in presence of competitive or noncompetitive inhibitor from the graph. Yes/No. Explain briefly why or why not C. Initial rate of reaction (v)
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