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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Find kcat for a reaction in which Vmax is 4 × 10-4 mol-min-1 and the reaction mixture contains one nanogram of enzyme. The molecular weight of the enzyme is 200,000 Da (1 Da = 1 g/mol). 2 x 10-13 min-1 2 x 10-11 min-¹ 80 min-¹ 8 x 107 min-¹ 8 x 10¹0 min-¹
At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)
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
What is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?
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
If you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.
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