Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 14P
The steady-state kinetics of an enzyme are studied the absence and presence of an inhibitor (Inhibitor A). The initial rate is given as a function of substrate concentration in the following table:
a. What kind of inhibition (competitive, uncompetitive. or mixed) is involved?
b. Determine Vmax and KM the absence and presence of inhibitor.
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The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function ofsubstrate concentration in the following table: (a) What kind of inhibition (competitive, uncompetitive, or mixed) isinvolved?(b) Determine Vmax and KM in the absence and presence of inhibitor.
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
The kinetics of an enzyme were measured as a function of substrate concentration in the
presence or absence of 10-4 M inhibitor. The following initial rate data were obtained:
Substrate (So µM/L)
3
5
Velocity (Vo, µmol/L-min)
Without inhibition
10
30
90
10.4
14.5
4.5
6.8
8.1
Is this a competitive or noncompetitive inhibition? Evaluate KM, KI, and Vmax. (HINT: use
linear regression to first estimate kinetic parameters for uninhibited and then for the
inhibited)
With inhibition
2.1
2.9
22.5
33.8
40.5
Chapter 8 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 8 - Prob. 1PCh. 8 - The enzyme urease catalyzes the hydrolysis of urea...Ch. 8 - An enzyme contains an active site aspartic acid...Ch. 8 - The folding and unfolding rate constants for a...Ch. 8 - In some reactions, in which a protein molecule is...Ch. 8 - Would you expect an “enzyme” designed to bind to...Ch. 8 - The initial rate for an enzyme-catalyzed reaction...Ch. 8 - a. If the total enzyme concentration in Problem 7...Ch. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - The following data describe the catalysis of...Ch. 8 - At 37 oC, the serine protease subtilisin has kcat...Ch. 8 - The accompanying figure shows three...Ch. 8 - The steady-state kinetics of an enzyme are studied...Ch. 8 - The same enzyme as in Problem 14 is studied in the...Ch. 8 - Enalapril is an anti-hypertension “pro-drug"...Ch. 8 - Initial rate data for an enzyme that obeys...Ch. 8 - Prob. 18PCh. 8 - Suggest the effects of each of the following...Ch. 8 - The inhibitory effect of an uncompetitive...Ch. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - In kinetics experiments, the hydrolysis of the...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- The same enzyme as studied in the presence of a different inhibitor (inhibitor B). In this case, two different concentrations of inhibitor are used. Data are as follows: (a) What kind of inhibitor is inhibitor B?(b) Determine the apparent Vmax and KM at each inhibitor concentration.(c) Estimate K1 from these data.arrow_forwardThe steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function of substrate concentration in the following table: v[(mmol/L)min- [S] (mmol/L) No inhibitor Inhibitor A 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 (a) What kind of inhibition (competitive, uncompetitive, or mixed) is involved? (b) Determine Vmax and Ky in the absence and presence of inhibitor.arrow_forwardThe characterization of an enzyme usually includes the determination of key kinetic parameters. Indicate which of the following statements are true. (This is a multi- select question ). KM is useful to when comparing different substrates, and how well they bind to the enzyme's active site. Kcat is a useful indicator of an enzyme's speed at 1/2 V Vm max is the maximal initial velocity of the enzyme when it is saturated with substrate. An enzyme is considered to approach "catalytic perfection" if it rarely makes an error. Enzymes are usually studied after boiling them in buffer, to remove the chance that contaminating microorganisms are responsible for the observed catalytic events.arrow_forward
- 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 approximationarrow_forwardNote the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell?arrow_forwardCompare 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.arrow_forward
- Kinetic data were gathered for Enzyme X, its substrate, and a known competitive inhibitor Z. Upon plotting the linearized kinetic data, one could surmise that the plot of the inhibited enzyme would have:a. a slope and y-intercept both lower in magnitude than the plot of the uninhibited enzyme using Eadie-Hofstee method.b. a constant slope and y-intercept that is lower in magnitude with the plot of the uninhibited enzyme using Eadie-Hofstee method.c. a slope and y-intercept greater in magnitude than the plot of the uninhibited enzyme using Hanes-Woolf method.d. a constant slope but a lower y-intercept than the plot of the uninhibited enzyme using Lineweaver-Burk method.arrow_forwardThe accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.arrow_forwardConsider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km and the type of inhibition based on the given data below Substrate concentration, uM 30 50 100 300 900 slope y-intercept Complete the table below (include correct units). Experiment A Vm Km Experiment A (Initial velocity without inhibitor, uM-min) Type of Inhibition: 10.4 14.5 22.5 33.8 40.8 Experiment B (Initial velocity with inhibitor, uM-min) 5.1 7.3 13.3 25.7 37.2 Experiment Barrow_forward
- Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderatearrow_forwardWhich of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.arrow_forwardGlucose can be isomerized to fructose to glucose isomerase. The enzyme kinetics of this enzyme was studied in the presence of an inhibitor X. Using the data provided, complete the table and determine what type of inhibitor is X. 1/ [S] , 1/M 1/V, w/o inhibitor Min/M 0.22 1/V, w/ inhibitor 0.33 0.27 0.2 0.16 0.20 0.14 0.13 0.16 0.11 0.11 0.14 0.09 0.11 0.13 Km/Vmax 1/Vmax Km Vmaxarrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License