The following data have been obtained for two different initial enzyme concentrations for anenzyme-catalyzed reaction.[E]=0.015 g/l)(g/l-min)[S](g/l)v([E]=0.00875 g/l)(g/l-min)1.1420.00.670.8710.00.510.706.70.410.595.00.340.504.00.290.443.30.392.90.352.5a. Find Kb. Find V for [E]=0.015 g/l.c. Find V for [E]=0.00875 g/l.d. Find k2.Use Eddie-Hostee plot to find your answer. Compare your result using Hanes-Wolf plot.

The Michaelis-Menten Kinetics and the Eddie-Hofstee PlotEnzyme-catalyzed reactions are fundamental…

Answered: The following data have been obtained…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

See similar textbooks

Similar questions

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:
Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.
The following reactions were catalyzed by an enzyme that follows the Michaelis-Menten mechanism in the absence and presence of inhibitor (10mM). Assume [E]T is the same for each reaction. Determine K, and/or K'. [S] (mM) Uninhibited v (um/s) Inhibited v. (um/s) 1 3 1.67 2 4.5 2.6 6.8 4.5 10 8.1 6.2 20 9.5 7.7
The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0
Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.
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
During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: E, () T(C) I (mmol/ml) S (mmol/ml) V (mmol/ml-min) 1.6 1.6 30 0.1 2.63 1.92 147 30 0.033 1.6 30 0.02 0.01 0.005 16 30 0.96 0.56 5.13 1.6 30 1.6 49.6 0.1 1.6 49.6 0.033 3.70 1.89 1.6 1.6 1,6 49.6 0.01 0.0067 49.6 1.43 49.6 0.005 LII 0.92 30 0.1 1.64 0.02 0.01 0.1 0.90 0.92 0.92 30 30 0. 0.58 0.92 30 0.6 0.92 0.92 30 30 0.6 0.6 0.033 0.02 1.33 0.80 0.57 a. Determine the Michaelis-Mentcn constant for the reaction with no inhibitor present at 30°C and at 49.6°C. b. Determine the maximum velocity of the uninhibited reaction at 30°C and an enzyme concentration of 1.6 g/l. c. Determine the KI for the inhibitor at 30*C and decide what type of inhibitor is being used.
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows: [S(u mol/L) v[(u mol/L) min-'] 5 22 10 39 20 65 50 102 100 120 200 135 (a) Estimate Vmax and K, from a direct graph of v versus [S]. Do you find difficulties in getting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better?
From the following data of an enzymatic reaction, determine the type of inhibition, the KM for the substrate and Ki for the enzyme-inhibitor complex. [S] mM 2.0 3.0 4.0 10.0 15.0 [P] mM/h (without inhibitor) 139 179 213 313 370 [P] mM/h ([I]=6mM) 88 121 149 257 313
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. ?maxVmax(μmol min−1) ?MKM(mM) Wild‑type 100 10 Mutant 1 0.1 Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1k−1 is much larger than ?2,k2, which of the following statements are correct? The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. ?0=V0=
Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.

SEE MORE QUESTIONS

Recommended textbooks for you

Human Anatomy & Physiology (11th Edition)

Biology

ISBN:

9780134580999

Author:

Elaine N. Marieb, Katja N. Hoehn

Publisher:

PEARSON

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Anatomy & Physiology

Biology

ISBN:

9781259398629

Author:

McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter

Publisher:

Mcgraw Hill Education,

Human Anatomy & Physiology (11th Edition)

Biology

ISBN:

9780134580999

Author:

Elaine N. Marieb, Katja N. Hoehn

Publisher:

PEARSON

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Anatomy & Physiology

Biology

ISBN:

9781259398629

Author:

McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter

Publisher:

Mcgraw Hill Education,

Molecular Biology of the Cell (Sixth Edition)

Biology

ISBN:

9780815344322

Author:

Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter

Publisher:

W. W. Norton & Company

Laboratory Manual For Human Anatomy & Physiology

Biology

ISBN:

9781260159363

Author:

Martin, Terry R., Prentice-craver, Cynthia

Publisher:

McGraw-Hill Publishing Co.

Inquiry Into Life (16th Edition)

Biology

ISBN:

9781260231700

Author:

Sylvia S. Mader, Michael Windelspecht

Publisher:

McGraw Hill Education

SEE MORE TEXTBOOKS