2. For each of the following sets of data draw the double reciprocal plot and answer the followingquestions: (be sure to pay attention to the various units)a. What type of inhibitor is it?b. What is Vmax and KM for the uninhibited enzyme?c. What is the Kcat for this enzyme? Is it an efficient enzyme?d. What is Kl and/or K'I for this inhibitor?V. (uM/sec) for 0.001 uM of Enzyme[S](mM)[1] = 0 mM[1] = 2 mM1.430.53153.331.43254.552.17405.713.08

Hi! Thank you for the question. We are authorized to answer two subparts at a time, since you have…

Answered: 2. For each of the following sets of…

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

Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and Km of the enzyme with no inhibitor. with inhibitor A, and with inhibitor B. [S] (uM) Vo (umol/min); w/ no inhib. Vo (umol/min); w/ inhib. A Vo (umol/min); w/ inhib. B 10 6.3 5.1 4.0 40 18.4 15.8 11.8 100 29.9 27.0 19.1 150 34.7 32.0 22.2 No inhib. Vmax= Km= Inhib. A Vmax= Km= Inhib. B Vmax= Km=
3. (a) The beakers below represent different conditions for measuring the initial velocity (vo) of an enzyme-catalyzed reaction under the steady-state approximation. The gray "donut-shaped" struc- tures represent the enzyme. The blue, filled circles represent free substrate molecules. The red cir- cles represent substrate molecules bound in the active site of the enzyme forming the Michaelis (ES) complex. Indicate in the diagram of the double reciprocal plot which kinetic parameters or variables each of the three "beaker conditions" represent either alone or in combination with another. A B 455 C V₁™¹ [So]-¹
What type of inhibition is being shown in the following graphs?
In pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does the inhibitor bind to E, ES or both? c. What is the effect of I on Vmax? d. What is the effect of I on Km?
Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4 µM but kcat doesn't change. Is the inhibitor competitive, uncompetitive, or mixed? And what are the value(s) of a and/or a'? Choose N/A if not applicable. Inhibitor = [ Select ] [ Select ] a = a'? = [ Select]
Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
-Inhibitor +Inhibitor [S] (mM) V0&νβσπ;(μmol/sec). νο&νβσπ: &ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITH iinhibitor?
The Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.
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?
1. As seen in the picture: - What kind of inhibition (competitive, uncompetitive, mixed) is involved? - Calculate Vmax and Kmax in the absence and presence of inhibitor A Show complete solution.
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?
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142

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