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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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.
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.
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
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?
The following data have been obtained for two different initial enzyme concentrations for an enzyme-catalyzed reaction. [E]=0.015 g/l) (g/l-min) [S] (g/l) v([E]=0.00875 g/l) (g/l-min) 1.14 20.0 0.67 0.87 10.0 0.51 0.70 6.7 0.41 0.59 5.0 0.34 0.50 4.0 0.29 0.44 3.3 0.39 2.9 0.35 2.5 a. Find K b. Find V for [E]=0.015 g/l. c. Find V for [E]=0.00875 g/l. d. Find k2. Use Eddie-Hostee plot to find your answer. Compare your result using Hanes- Wolf plot.
Calculate 1/[S] and 1/V to complete the table. Use this data to draw a Lineweaver-Burke plot, with lines for ‘no inhibitor’ and ‘with inhibitor’. Be sure to label your axes and lines. What kind of inhibitor is it? Estimate Vmax and Km for the uninhibited reaction.

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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