Pearson eText for Biochemistry: Concepts and Connections -- Instant Access (Pearson+)
Pearson eText for Biochemistry: Concepts and Connections -- Instant Access (Pearson+)
2nd Edition
ISBN: 9780137533114
Author: Dean Appling, Spencer Anthony-Cahill
Publisher: PEARSON+
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Chapter 8, Problem 7P

The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows:

Chapter 8, Problem 7P, The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate

  1. Estimate Vmax and KM from a direct graph v versus [S]. Do you find difficulties in getting clear answers?
  2. Now use a Lineweaver-Burk plot to analyze the same data. Does this work better?

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A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of substrate concentration in the presence and absence of 0.001μM inhibitor. She obtains the following data. What is the Vmax and Km for the "no inhibitor" and "+ inhibitor" experiments. Ans, What would be value of V0 for the "+inhibitor" at [S] = 0.4μM and the inhibitor is most likely a competitive, uncompetitive or mixed inhibitor.
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.
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where v 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 (ro) at different substrate concentrations ([S]). 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- Vmax= µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 75 50 Km = 25 K 0 10 20 30 V max 40 50 [S] (M) 1/2 V max Michaelis-Menten curve 60 70 80 90 100 HM
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