The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where u is the velocity, or rate, Vmax is the maximum velocity, K., is the Michaelis Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (U) at different substrate concentrations ([S]). V= First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position. Estimate the values for Vmax and Km. V max = µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 Km = 75 50 25 0 K m 0 10 20 30 V max 40 50 [S] (μM) 1/2 V 60 Michaelis-Menten curve max 70 80 90 100 μM

The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where u is the velocity, or rate, Vmax is the maximum velocity, K., is the Michaelis Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (U) at different substrate concentrations ([S]). V= First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position. Estimate the values for Vmax and Km. V max = µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 Km = 75 50 25 0 K m 0 10 20 30 V max 40 50 [S] (μM) 1/2 V 60 Michaelis-Menten curve max 70 80 90 100 μM

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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The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the reciprocal of the substrate concentration (1/[S]), is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km. What term is represented by C? Linewegver-Burk Pt 1/Vmax O A. В. -1/Km Km/Vmax C.
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:
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.
The Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.
Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: (a) Lineweaver-Burk equation is a manipulation of the Michaelis-Menten equation. Give the equation and state why it is necessary. (b) Is high or low Vmax preferable for an enzyme reaction? Give reason.
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.
In enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.
In enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.
How is the Michaelis constant defined, and what does a low or high value for Km tell you? What is the difference between the velocity and initial velocity of an enzyme reaction? What determines the efficiency of an enzyme reaction, and what terms are used to describe it?
Given the assumption used to derive the Michaelis-Menten equation for enzyme kinetics that the back reaction from P + E back to ES does not occur, why is it important in measuring experimental data for Michaelis-Menten analysis to determine the initial rate of the reaction just after adding substrate to the sample being measured? O Because faster rates can be measured more accurately than slower rates later in the process. Because the Michaelis-Menten equation also contains the position of the equilibrium of the reaction. ● By using this approach, the amount of P at the start of the experiment is extremely low, causing the back reaction to be essentially absent. Because in this way the [ES] concentration has not yet reached steady state.
The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical 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.