1. For enzyme catalyzed reaction:kiS + E=X (fast)k2X -2> P + E (slow)derive the rate law and answer the following:a) What is meant by Michaelis-Menten constant km?(b) Prove that order of reaction in substrate changes from unity to zero athigher [S].(c) What is the rate and value of km, if k2 >> k1.(d) Draw the potential energy diagram for enzyme catalyzed reaction.

Since you have posted a question with multiple subparts, we will solve the first three sub-parts for…

Answered: 1. For enzyme catalyzed reaction: ki S…

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

Imagine a typical enzyme kinetic curve of [S] vs. V. The maximum [S] is about four times the Km. Lines are drawn at [S] = Km and V = Vmax. The asymptote is drawn at [S] = 0. 1. What effect does altering Km have on Vmax? Explain. 2. What effect does altering [E] have on Km? Vmax? Explain. 3. At what concentration of [S] is the initial velocity proportional to [E]? Explain.
What are the benefits of measuring the initial rate of a reaction Vå for use in kinetic studies? (This is a multi-select question). [ES] can be measured accurately. changes in [S] are negligible, so the value of [S] is known. changes in Km are negligible, so Km can be treated as a constant. V₁ = Vmax. --> A negligible amount of product has formed, so that the back reaction P -- need not be considered. ES
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
e) Two 20th century scientists, Leonor Michaelis and Maud Leonora Menten, proposed the model known as Michaelis-Menten Kinetics to account enzymatic dynamics. The model serves to explain how an enzyme can cause kinetic rate enhancement of a reaction and explains how reaction rates depends on the concentration of enzyme and substrate. k1 k2 E + S= ES → E + P k-1 Equation 1 i. Prove Equation 2 by referring to Equation 1. Vmax[S] V = [S] + KM Equation 2 ii. Give three characteristic features of catalyst.
The value of Vmax for an enzyme-catalyzed reaction: A) most often reflects the chemical steps of catalysis B) can be determined from initial velocities that are linear with respect to substrate concentration OC) is limited only by the amount of substrate supplied D) can be converted to kcat/Km by accounting for the enzyme concentration OE) is higher for enzymes that also exhibit higher Km values
Sketch a typical enzyme kinetic curve of [S] vs. V. The maximum [S] should be about four times the Km. Draw lines at [S] = Km and V = Vmax. Draw the asymptote at [S] = 0.
the kinetics of an enzyme were analyzed in the absence of inhibitors, as well as in the presence of inhibitor A and inhibitor B. Using the given data below, construct or calculate the following (make sure the label graphs with appropriate axes and equations, and circle final answers) plot 1[S] as abscissa and 1/v as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots Calculate the; Km of enzyme in the reaction without inhibitor Km of the enzyme in the reaction with inhibitor (A dnB) Vmax of the uninhibited reaction Vmax of the inhibited reaction (A and B) What kind of inhibitor (A and B) was added to the enzyme-catalyzed reaction? Explain in terms of changes in Km and Vmax
In the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1
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.
Solve the Michaelis-Menten equation for KM when vo=Vmax/2. What does this tell you about the relationship between substrate concentration and enzymes with high KM values? With low KM values?
For some Enzyme, the Vmax is 18 micromols/min, Km is 400 microM. If the substrate concentration is 100 microM, what is the velocity of the reaction?
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the Km to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? 0.09 MS-1 O 0.133 Ms-1 O 0.18 Ms ¹ 9 Ms-1 O 0.018 Ms-1 0.2 MS-1

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