The table below contains experimental data for theenzyme A; substrate concentration (mM) and initialvelocity (mM/min). Plot a suitable graph andcalculate the Km and Vmax for this enzyme. In2.your answer, insert an image of the graphand show your calculations.Substrate concentration; [S] (mM) Initial Velocity; Vo (mM/min)10.0033.335.0020.003.3314.292.5011.11

The Michaelis-Menten equation is used for calculating and analyzing the reaction enzyme kinetics.…

Answered: The table below contains experimental…

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

You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol L-1
Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over number
Draw the Michaelis-Menten Plot and Lineweaver-Burke Plot of an enzyme in thefollowing situation. An enzyme, Enzyme A, has an optimal temperature at 34.5oC. The enzyme kinetic parameters were recorded to be Km = 15.0 μM, Vmax = 12.0 μM/s. The condition for an enzyme kinetic experiment has the temperature raised to 36.5oC. What will happen to the results? Provide at least five data sets prior to raising the temperature and after raising the temperature and plot the graphs as overlaying figures for comparison. Explain youranswer using a minimum of 200 words.
You measure the kinetics of an enzyme as a function of substrate concentration using the Lineweaver-Burke equation. The enzyme concentration is maintained constant at a level of 1 μM. From these data, determine the equation of the line, Vmax, KM, and kcat for the enzyme. [S], μM Velocity, μM/min 2 2.9 3 3.8 4 4.4 5 5.0 6 5.4 7 5.8 8 6.2 9 6.4 10 6.7 The Lineweaver-Burke equation is 1V=1V= __________ (1/|S|) + _________. Therefore, the Vmax is __________ μM/min, KM is ___________ μM, and kcat is ___________ /min.
The following were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Reaction Velocity (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 20 652 1000 The Km for this enzyme is approximately _____________. (Round to the nearest integer)
Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol/L. Upload your tabulated answers and show your calculations.
The Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the reaction of the reaction when the substrate concentration is 7 × 10−2 mmol/min? a. 35 mmol/min b. 50 mmol/min c. 60 mmol/min d. 70 mmol/min
Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km?
Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:
An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?
An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 μM and a kcat value of 206 s−1 . At an initial enzyme concentration of 0.0100 μM , the initial reaction velocity was found to be 1.07×10−6 μM/s . What was the initial concentration of the substrate, [S] , used in the reaction ? Express your answer in micromolar to three significant figures..

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