Table 1. Kinetic parameters of a chosen model wild-type (WT) enzyme and threecatalytically-improvedmutants (M1 to M3).Enzyme variantsk (8¹)WTMIM2M350500100050K₁, (μM)101001001k/K (HM¹¹ s¹)5The study above was done on a wildtype enzyme and three genetically-engineeredmutants. The purpose was to find a mutation to improve the catalytic efficiency of theenzyme for industrial use. Which is the most accurate statement concerning the data?M2 is the optimal choice when substrate concentrations are saturating.The wildtype enzyme is still preferable to M3 when S<

INTRODUCTION : Wild type Enzyme - These are the enzymes which are found naturally and are not…

Answered: The study above was done on a wildtype…

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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Similar questions

In a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
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
PLP can catalyze both \alpha, \beta elimination reactions and \beta, \gamma - elimination reactions. Propose a mechanism for the following PLP - catalyzed \beta, \gamma elimination
The figure below shows the dependence of the enzyme's rate, v (in µM/min), as a function of substrate concentration, S (in mM). Also shown is the dependence of the rate in the presence of an inhibitor, present at a concentration of 0.2 mM. Based on this information, which of the following does this inhibitor most likely interact with? 1/v 1- 05 1/[S) O A. Michaelis complex O B. [E O C. free enzyme O D. free substrate O E. Both "A" and "B."
Which of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
From a series of flasks with a constant concentration of enzyme the following initial velocities weretaken, they were obtained as a function of the concentration of the substrate.a) Calculate the KM and Vmax kinetic parameters of the three forms (Lineweaver-Burk, Eadie-Hofstee, Dixon).b) Analyze which are the atypical data that cause a low correlation, which can be eliminated and explain youranswer.
Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?
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?
An enzyme with a Km of 3X10-5 M has a lower affinity for its substrate than an enzyme with a Km of 2x10-6 M. Is this true or false?

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