Using linear regression analysis, determine the values of Vmax and KM of the enzyme inthe PRESENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units)VmaxKM =!3!What is the MODE of inhibition exerted by DEDS? You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newlydiscovered enzyme known as BILISTASE. The kinetics data are shown below:[Substrate, uM)Vo with DEDS (uM/min)Vo without DEDS (uM/min)1.6671.6003.5442.5001.9234.2593.3332.1394.73714.0002.2685.0195.0002.4105.336Using linear regression analysis, determine the values of Vmax and KM of the enzyme inthe ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units)VmaxKM

Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Answered: Using linear regression analysis,…

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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Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
you are trying to come up with a drug to inhibit the activity of an enzyme thuogth to have a role in a liver disease. in the lab the enzyme was shown to have a Km of 1x10-6 M and Vmax of 0.1 micromoles/min.mg measruing at room temperature. you developed a mixed non-competitve inhibitor with a ki=0.4x10-6M and a Ki` pf 0/2 x 10-5 What will be the apparent Km in the presence of 1.0x10-6 M?
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
(a) You are given the following experimental measurements for the effects of an inhibitor on the initial velocity of an enzymatic reaction. Plot the data and determine what type of inhibition is being observed. Label all axes. [S] (MM) Vo (mM • Vo with I present (mM ⚫s-¹) 1 2.8 3 6.0 1.0 2.5 4 7.0 3.1 8 9.9 12 11.5 4.8 5.7 (b) Briefly explain how varying [S] can be used to determine whether an inhibitor is uncompetitive or competitive. Be sure to include in your explanation why this method would work.
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches/Vm Vmax 2α' Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
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.
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."
If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
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.
a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your work
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?

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Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the PRESENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units)