After purifying alkaline phosphatase, you perform enzyme kinetic experiments with andwithout an inhibitor to obtain the following plot:With inhibitorWithout inhibitor1/V (1/mM min?)0.30.2-150 -100 -5050 100 150 200 250 3001/s (1/mM)a) What is the name given to this type of enzymatic plot?b) Using the graph, calculate K_ and V_inhibitor. Show all calculations.for the enzyme, with and without themax

Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Answered: After purifying alkaline phosphatase,…

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

Given the line-weaver Burke plot below for Enzyme Y, identify the Vmax for Enzyme Y. -10 30 1/v 1/[S] 5 10 Enter the numerical value for Vmax only, no letters or symbols. Round answer to 2 significant figures.
What would be the correct answer to this problem?
Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.
Given the following set of kinetic data, what is the KM of the enzyme? Numerical answer, only (assuming the same units as seen in the table). [S] (micro M) vo (Micro mol/sec) 1 49 2 96 8 249 50 498 100 656 1000 778 5000 999
Please answer A & B attached with image.
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
The following data were collected for an enzyme that can be described by Michaelis Menton kinetics. Use graphical analysis to determine the Km and Vmax for this exzyme / substrate combination. [S] mM Product formed (umol/min) 0.21 1.5 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45
Do not give handwriting solution.
At steady state,[Es} stays the same although substrate concentraion is steadily decreasing and product concentraion is increasing .how do you explain this?
At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate at one-tenth of its maximum rate? Assume the enzyme obeys Michaeli s-Menten kinetics.
From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
what concentration of a competitive inhibitor is required to yield 60% inhibition of an enzyme at a substance concentration of 1.0x10^-4 M. The Km for the enzyme is 22 uM and the Ki for the inhibitor is 59 uM. To what concentration must the substrate be increased to reestablish velocity at the uninhibited value?

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

After purifying alkaline phosphatase, you perform enzyme kinetic experiments with and without an inhibitor to obtain the following plot: With inhibitor Without inhibitor 1/V (1/mM min) 0.3 0.2 -150 -100 -50 50 100 150 200 250 300 1/s (1/mM)