Enzyme X has a Km for substrate A which is twice as large as its Km...
Enzyme X has a Km for substrate A which is twice as large as its Km for substrate B. If the enzyme is added to a solution containing equal, but low concentrations of A and B and Vmax for A and B are equal:
substrate A will be used at a rate equal to substrate B
substrate A will be used at a rate greater than substrate
substrate B will be used at a rate greater than substrate A.
substrate A will be used exclusively.
Homework Answers
Km is the substrate concentration when the rate of reaction (Vo) is equal to half of the Vmax, lower Km means the at lower concentrations of the substrate the rate of reaction is high, here Km of B=Km of A/2, that is Km of B less than the Km of A and Vmax of both reactions are same so at lower concentrations substrate B will be used at a greater rate than substrate A. so the answer is substrate B will be used at a rate greater than substrate A.
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Enzyme X has a Km for substrate A which is twice as large as its
Km...
Consider an enzyme with the following properties: – Km = 0.0050 M At what substrate conc....
Consider an enzyme with the following properties: – Km = 0.0050 M At what substrate conc. would the enzyme operate at one-fourth of its maximum rate? At a given substrate conc. (e.g., ½Km) what would the rate be as a fraction of Vmax?
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
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yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
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At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
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3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed to have an initial rate Vo = 0.75 Vmax. Select one: O a. [S] = 0.33 x km O b. [S] = 0.25 km O c. [S] = 0.75 x Km O d. [S] = 0.3 x km O e. [S] = 0.5 x km Check Next page ime Jump to...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
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