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 8P
a. If the total enzyme concentration in Problem 7 was 1 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute?
b. Calculate kcat/ KM for the enzyme reaction in Problem 7. Is this a fairly efficient enzyme? (See Table 8.5.)
7. The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows:
- Estimate Vmax and KM from a direct graph v versus [S]. Do you find difficulties in getting clear answers?
- Now use a Lineweaver-Burk plot to analyze the same data. Does this work better?
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Check out a sample textbook solutionStudents have asked these similar questions
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP.
Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme.
1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase.
Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
Shown below are Km, and Vmax values obtained for an enzyme A which catalyze the transformation of
the following substrates. Enzyme concentration used was 0.01 M.
Km, mM
0.02
Vmax, mM/min
5.3
Substrate
1
2
1.5
13.7
3
2.6
100
4
0.1
25
0.05
62
1. Which substrate have the highest affinity for the enzyme? Explain.
2. Which will show higher efficiency of converting the substrate to the product? Show solutions and
еxplain.
Consider an enzyme that follows standard
Michaelis-Menten kinetics and has the following
kinetic constants:
%3|
k2 = 1.5 x 10? s1
Еo 3D 1 х 104 М
= 1 x 104 M
a. What is the value of the maximum
rate VM?
b. Prepare a hand-drawn quantitative
plot on graph paper (not a simple
sketch nor an EXCEL-generated graph)
of the enzymatic reaction rate versus
substrate concentration (like Fig 3-3)
using the kinetic parameters given
above. Be sure to label the axes and
include numeric values on the axes.
C. Based upon your hand drawn
saturation plot, at what substrate
concentration is the enzymatic
reaction rate 75% of Vm?
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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- Consider 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_forwardThe change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the table below. Determine the Vmax and Km of the enzyme in the absence and presence of C. Is C an inhibitor or an activator of enzyme A? Determine the type of inhibition or activation. Rate of formation of Product B in the presence of 25 mg/mL C (mM/min) Substrate Rate of formation of (mM) Product B (mM/min) 0.5 21.5 14.1 1 30.2 22.2 1.5 34.9 27.0 2.5 39.8 33.1 3.5 42.0 36.3arrow_forward(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90arrow_forward
- a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your workarrow_forwardGiven the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.arrow_forwardExplain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.arrow_forward
- Please see the attached image.arrow_forwardThe 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 40.5arrow_forwardThe 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.arrow_forward
- An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :arrow_forwardSketch and label a plot showing the enzyme's initial velocity relative to pH over the pH range 4 - 9 for the enzyme-catalyzed reaction under these two conditions: A. The substrate concentration is very, very high. B. The substrate concentration is less than the enzyme's Km.arrow_forward(a) If the total enzyme concentration 1 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute?(b) Calculate kcat/KM for the enzyme reaction. Is this a fairly efficient enzyme? (as shown.)arrow_forward
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