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.
Add Answer to:
Enzyme X has a Km for substrate A which is twice as large as its
Km...
1. Michaelis and Menten examined how the velocity of enzyme catalyzed reactions change with substrate concentration....
1. Michaelis and Menten examined how the velocity of enzyme catalyzed reactions change with substrate concentration. Which of the following is (are) common to all enzyme catalyzed reactions? Velocity is insensitive to changes in [substrate] at all substrate concentrations. Km is the [substrate] required to reach 50% of Vmax. Velocity is responsive to changes in [substrate] when the Km > [substrate]. Velocity is insensitive to [substrate] when [substrate] is much greater than Km. Velocity reaches 90% of Vmax when [substrate]...
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]...
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed...
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...
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...
A. Prove that Km equals the substrate concentration at ½ Vmax . (Show solution) B. Why...
A. Prove that Km equals the substrate concentration at ½ Vmax . (Show solution) B. Why do structural analogs if the transition-state intermediate of an enzyme inhibit the enzyme competitively and with low Ki values (binds tightly)?
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity...
If the enzyme concentration is 3.8 X 10-8, what concentration of substrate would generate a velocity equal to 0.25 Vmax? Km is not needed. Km= 15.42M
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)
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)
The enzyme that hydrolyzes acetylcholine to form acetate and choline has a Km = 9 x...
The enzyme that hydrolyzes acetylcholine to form acetate and choline has a Km = 9 x 10-5 M for the substrate. In an reaction flask with 5 nanomol / mL of the enzyme and 150 µM of acetylcholine, an initial reaction rate of 40 µmol / mLs was observed. a) Calculate vmax for this amount of enzyme. b) Calculate kcat for the enzyme. c) Calculate the catalytic efficiency of the enzyme. d) Does this enzyme approach “catalytic perfection?
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...
Most questions answered within 3 hours.
-
Where is the error in this code sequence?
String s1 = "Hello";
String s2 = "ello";...
asked 10 months ago -
Financial data for Joel de Paris, Inc., for last year
follow:
Joel de Paris, Inc.
Balance...
asked 10 months ago -
Consider this reaction:
Al2(SO4)3 (aq)+ BaCl3
(aq) Al2Cl6 (aq)- +
3BaSO4(s) . What is the...
asked 10 months ago -
Suppose that Savneet is considering increasing her
recent random sample from 20 car rentals to 40...
asked 10 months ago -
Trucks arrive at an unloading terminal at an average rate of 120
per hour.
Trucks arrive...
asked 10 months ago -
Why are methanol and ethanol completely soluble in water while
octanol is not very little soluble....
asked 10 months ago -
A facilities manager at a university reads in a research report
that the mean amount of...
asked 10 months ago -
When the CuSO4 is rehydrated by adding water to the anhydrous
compound, is this an endothermic...
asked 10 months ago -
A ray of sunlight is passing from diamond into crown glass; the
angle of incidence is...
asked 10 months ago -
A block of mass 0.249 kg is placed on top of a light, vertical
spring of...
asked 10 months ago -
how do the kidneys compensate in the presences of acidosis
a) trigger hyperventilate
b) reserve acid...
asked 10 months ago -
Question 501 pts
The rental rate of capital to the firm increases. Which of the
following...
asked 10 months ago