Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all thestatements that are true.WithoutenzymeWithenzymeA+BTimeABOa. The reaction is now spontaneous due to the addition of enzymeb. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reactionO C. The reaction is exergonicO d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to theuncatalyzed reactione. The enzyme stabilizes the transition state for the reactionReleased Energypes

Those proteins or biological catalysts which help to speed up the chemical reaction are termed…

Answered: Consider the following free energy…

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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Explain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?
At what substrate concentration would an enzyme with a Km of 0.005M operate at one quarter of its Vmax? What would be the Km for an enzyme if it is operating at 90% of its Vmax when the substrate concentration is 0.01M
Which of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.
Describe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.
For an enzyme that has a Km of 25 mM, Vmax of 50 mM/s and kcat of 250 s-1, how long does a single reaction take? Select one: 50 ms 250 ms 4 ms 25 s 4 s
Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energy
Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Define Vmax and KM in the equations.
Draw and label the rate law graph for an allosteric enzyme? Give an explanation for the shape of the curve.
An uncatalyzed reaction progresses at a rate of 20micromoles per minute while the same reaction in the presence of an enzyme progresses at a rate of 100micromoles per second. What is the rate enhancement achieved by the presence of the enzyme? At 25oC, how much energy is required to produce a 10-fold rate enhancement? At the same temperature, how much energy is required to produce a million-fold rate acceleration?

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Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme pes