Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 6, Problem 81TQ
Summary Introduction
To review:
For the equation of competitive inhibition:
a) The value of α can ever be less than 1 is to be determined.
b) The consequence for the value of α less than 1 is to be explained.
Introduction:
In the process of competitive inhibition, the inhibitor competes with the substrate for the substrate-binding site of the enzyme. This is because the binding of the substrate and the inhibitor occurs at identical sites. The inhibitor is structurally similar to the substrate. The net result is that the enzyme binds indiscriminately with the inhibitor and is not available to the substrate.
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The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3.
CO2 + H20 > H+ + HCO3
There are many different isoforms of this enzyme. (see for instance
http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3.
CO2 + H20 > H+ + HCO3
There are many different isoforms of this enzyme. (see for instance
http://en.wikipedia.org/wiki/Carbonic_anhydrase . Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.
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.
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
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