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

See similar textbooks

Similar questions

A purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
The above graphs (Lineweaver-Burk) were plotted using data from an experiment that investigated changes in initial velocity, V0, (in mmol/min) as a function of substrate concentration, [S], (in mmol/L) for an enzyme-catalysed reaction. The initial velocity was measured at a fixed concentration of enzyme at different concentrations of substrate in the absence of any inhibitor and was then repeated in the presence of a competitive inhibitor at two different concentrations. Use the graph to determine the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the reaction with (i) the lower level of inhibitor and (ii) the higher level of the inhibitor. TEMPLATE FOR ANSWERS Vmax of uninhibited reaction Intercept on y-axis = = __________________ Vmax = __________________ Km value of the uninhibited reaction Intercept on x-axis = =…
A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: [Substrate] (mM) Vo (mM/min) (without inhibitor) Vo (mM/min) (with inhibitor) 15 1.11 0.67 30 1.81 1.17 45 2.28 1.56 60 2.62 1.88 90 3.09 2.36 Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor. y-int [ Select ] slope [ Select] • Vmax (Sclect] mM/min Km [ Sclect) mM
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?
Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
What are the meanings and differences between Ki, Km, and ĪC50? Are there certain advantages or disadvantages when measuring Ki and IC50 in terms of enzyme activity?
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.
A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: Vo (mM/min) (without inhibitor) Vo (mM/min) (with inhibitor) [Substrate] (mM) 15 1.11 0.67 30 1.81 1.17 45 2.28 1.56 60 2.62 1.88 90 3.09 2.36 Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the ab- sence of an inhibitor. - y-int = - slope = - vmax = - Km =
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 =

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

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)