---**Understanding Lineweaver-Burk Plots****The figure is a Lineweaver-Burk plot. Which of the following is equal to the x-intercept in a LB plot? Choose the one best answer.**- ( ) -Km/Vmax- ( ) 1/Vmax- ( ) 1/Km- ( ) -1/Vmax- ( ) -1/Km **(Correct Answer)****Explanation of the Diagram:**The Lineweaver-Burk plot, also known as the double reciprocal plot, is a graphical representation of the Lineweaver-Burk equation of enzyme kinetics. In this type of plot, the reciprocal of the reaction rate (1/V) is plotted against the reciprocal of the substrate concentration (1/[S]). **Key features of the plot include:**- **Y-axis (vertical):** 1/V (reciprocal of reaction velocity)- **X-axis (horizontal):** 1/[S] (reciprocal of substrate concentration)- The y-intercept of the plot equals 1/Vmax.- The x-intercept is equal to -1/Km.In the given problem, the correct answer to the question about what the x-intercept represents in a Lineweaver-Burk plot is "-1/Km".**Educational Importance:**Understanding the Lineweaver-Burk plot is essential for analyzing enzyme kinetics. By interpreting the intercepts, one can determine important kinetic parameters, such as Km (Michaelis constant) and Vmax (maximum reaction velocity), which provide insights into enzyme affinity and catalytic capabilities.---This transcription provides a clear explanation suited for an educational website, detailing the elements of the plot and emphasizing the importance of understanding these concepts in enzyme kinetics. **Understanding the Lineweaver-Burk Plot in Enzyme Kinetics**The Lineweaver-Burk plot is a graphical representation of enzyme kinetics, allowing for a clear visualization of key parameters in enzyme-catalyzed reactions. ### Diagram ExplanationThe plot depicted is a double reciprocal transformation of the Michaelis-Menten equation and graphs 1/v (reciprocal of velocity) against 1/[S] (reciprocal of substrate concentration). Key elements in the diagram include:- **X-axis:** 1/[S] (reciprocal of substrate concentration)- **Y-axis:** 1/v (reciprocal of reaction velocity)- **Y-intercept:** Represents 1/Vmax, where Vmax is the maximum reaction velocity.- **X-intercept:** Represents -1/Km, where Km is the Michaelis constant.- **Slope:** The slope of the line is Km/Vmax.### Sample Question**Question:**The figure is a Lineweaver-Burk plot. Which of the following is equal to the x-intercept in a Lineweaver-Burk plot? Choose the one best answer.- ○ -Km/Vmax- ○ 1/Vmax- ○ 1/Km**Answer:**- The correct answer is: **-1/Km**Understanding these parameters is crucial for interpreting enzyme kinetics and for applications in biochemistry and pharmacology.

Lineweaver Burk plot : Graphical representation of enzyme kinetics. X-axis : reciprocal of…

Answered: 1/[S] The figure is a Lineweaver-Burk…

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

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molecule A Plot of velocity versus substrate B Lineweaver-Burk plot 1/v Km 1 Vmax (S) Vmx 1 V max 1/2Vmax 1/Vmax -1/Km Km [S] 1/[S] fppt.com molecule Exercise The following data describe an enzyme-catalyzed reaction. Plot these results using the Lineweaver-Burk method, and determine values for KM and Vinax- The symbol mM represents millimoles per liter; 1 mM = 1 × 10 3 mol L. (The concentration of the enzyme is the same in all experiments.) Velocity (mM sec-) Substrate Concentration (тм) 2.5 0.024 5.0 0.036 10.0 0.053 15.0 0.060 20.0 0.061 fppt.com
Compare and contrast Bound Fraction equation in ligand binding and Michaelis-Menten equation in enzyme kinetics, including their double-reciprocal forms. Discuss what Km is important for and what Vmax (or kcat) is important for? Under what (substrate) conditions is Km more important than Vmax, and under what (substrate) conditions is Vmax more important than Km? Based on the discussions in question 2, explain what type of inhibitors works best under (a) high substrate concentration and (b) low substrate concentration.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E + S ES → E + P. The model can be more readily understood when comparing three conditions: [S] > Km- Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions Almost all active sites will [ES] is much lower than [Efree]. be filled. The rate is directly proportional to Increasing [Etotal] will increase [S]. Km: Adding more S will not increase [Efree] is equal to [ES]. the rate.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% for an enzyme-catalyzed, single-substrate reaction E + S=ES → E + P. The model can be more readily understood when comparing three conditions: [S] > Km- Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions [ES] is much lower than [Efree]. Reaction rate is independent of Increasing [Etotal] will lower Almost all active sites will Km- be filled. [S). [Efree] is about equal to [Etotal]. Show All W- 5179933 (3).docx 5179933 (4).docx PCR-MINI RES....docx MacBook Pro
For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M
The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V₁ for an enzyme-catalyzed, single-substrate reaction E + S ⇒ ES →→ E + P. The model can be more readily understood when comparing three conditions: [S] > Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Almost all active sites will be filled. Adding more S will not increase the rate. Answer Bank Not true for any of these conditions Increasing [Etotal] will lower Km.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction E + SES →E + P. The model can be more readily understood when comparing three conditions: [S] > Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V, where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Reaction rate is independent of [S]. Not true for any of these conditions The rate is half of the maximum rate.
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? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?
Quantum tunneling appears to play a significant role in the facilitation of efficient enzyme catalysis in reactions involving the transfer of protons and hydride ions. Provide an energy diagram for a hypothetical reaction in the presence and absence of an enzyme that illustrates the tunneling process.
Many enzyme -catalyzed reactions are consistent with a modified version of the Michaelis -Menten mechanism in which the second step is also reversible. For this mechanism obtain an expression for the rate of formation of product and find its limiting behavior for large and small concentrations of substrate using steady state approximation
Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111…

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1/[S] The figure is a Lineweaver-Burk plot. Which of the following is equal to the x- intercept in a LB plot? Choose the one best answer. -Km/Vmax 1/Vmax 1/Km O-1/Vmax 0-1/Km