Microbiology: An Introduction (13th Edition)
13th Edition
ISBN: 9780134605180
Author: Gerard J. Tortora, Berdell R. Funke, Christine L. Case, Derek Weber, Warner Bair
Publisher: PEARSON
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Chapter 5, Problem 3R
DRAW IT An enzyme and substrate are combined. The
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Label the x axis in each graph below with the appropriate factor (possible factors: temperature, pH, substrate concentration at constant enzyme concentration, enzyme concentration at constant substrate concentration) so that the effect of this factor will be illustrated correctly.
Below is data collected from an experiment that examined the activity of Enzyme A at three
different temperatures. The amount of product formation was measured in mg/min.
Cold Enzyme
Room Temp Enzyme
Boiled Enzyme
3 mg/min
10 mg/min
A mg/min
Based on the above results:
What is the optimal environment for this enzyme?
Describe in detail what most likely happened to the enzyme in the boiled temperature.
An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results
obtained are summarized in the table below.
In all the experiments, the concentration of the enzyme is the same.
Substrate Concentration
Velocity
(pmol/min)
(pmol)
1.5
0.21
3
0.28
4
0.32
0.36
8
0.4
15
0.45
18
0.47
1. Plot or graph these results using the Lineweaver-Burk method.
2. Determine the KM and Vmax values. Show all equations and calculations.
Chapter 5 Solutions
Microbiology: An Introduction (13th Edition)
Ch. 5 - Prob. 1RCh. 5 - DRAW ITUsing the diagrams below, show each of the...Ch. 5 - DRAW IT An enzyme and substrate are combined. The...Ch. 5 - Define oxidation-reduction, and differentiate the...Ch. 5 - There are three mechanisms for the phosphorylation...Ch. 5 - All of the energy-producing biochemical reactions...Ch. 5 - Fill in the following table with the carbon source...Ch. 5 - Write your own definition of the chemiosmotic...Ch. 5 - Why must NADH be reoxidized? How does this happen...Ch. 5 - NAME IT What nutritional type is a colorless...
Ch. 5 - Which substance in the following reaction is being...Ch. 5 - Which of the following reactions produces the most...Ch. 5 - Prob. 3MCQCh. 5 - Which of the following compounds has the greatest...Ch. 5 - Prob. 5MCQCh. 5 - Prob. 6MCQCh. 5 - Which culture produces the most lactic acid? Use...Ch. 5 - Which culture produces the most ATP? Use the...Ch. 5 - Which culture uses NAD+? Use the following choices...Ch. 5 - Which culture uses the most glucose? Use the...Ch. 5 - Explain why, even under ideal conditions,...Ch. 5 - The following graph shows the normal rate of...Ch. 5 - Compare and contrast carbohydrate catabolism and...Ch. 5 - How much ATP could be obtained from the complete...Ch. 5 - The chemoautotroph Acidithiobacillus can obtain...Ch. 5 - Haemophilus influenzae requires hemin (X factor)...Ch. 5 - The drug Hivid, also called ddC, inhibits DNA...Ch. 5 - The bacterial enzyme streptokinase is used to...
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- At what temperature in the above graph is the enzyme the most active?arrow_forwardThe diagram shows the mechanism of a general enzyme‑catalyzed reaction. Put the labels in the correct locations. The abbreviations E, P and S indicate the enzyme, product, and substrate, respectively.arrow_forwardThe order of the data in the table is reversed. Pay attention and calculate straight. Some experiments have been done using a fixed amount of enzyme. Made in different substrate concentrations. The table below contains data. S( mM/L-min) V( mM/L-min) 2000 155 1000 150 200 120 100 100 60 80 40 64 20 40 10 20 Find Vmax and Km using all data points and at least two linear transformationsarrow_forward
- Here’s a kinetic model for some enzyme E acting on substrate S. The last step (EP → E) is rate determining. Write an equation for the rate of the reaction. And write an equation for the total amount of enzyme in this system.arrow_forwardWhich of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.arrow_forwardWhich of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active sitearrow_forward
- an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form Carrow_forwardAn allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %arrow_forwardWhich of the following statements is true about effect of substrate concentration on enzyme activity ? The rate of reaction increases as the substrate concentration increases up to certain limit at which the reaction rate is maximal (Vmax.) At Vmax, the enzyme is completely saturated with the substrate, At Vmax, any increase in substrate concentration don't affect the reaction rate. All of themarrow_forward
- Please select all of the following statements that are true. Cofactors involve the use of vitamins to assist enzymes Competitive inhibitors bind to the same active site as the substrate. When the substrate binds to the enzyme the reaction rate increases. Non-competitive inhibitors can act as both inhibitors and activators.arrow_forwardAn enzyme-catalyzed reaction has a Km of 4 mM and a Vmax of 5x10-3 uM/s. What is the reaction velocity when the substrate concentration is: 5 mM 4 mMarrow_forwardlace the description with the appropriate step in the enzymatic reaction. The enzyme changes shape, resulting in an induced fit between substrate and enzyme. Glucose and galactose are released, and the enzyme is free to bind other substrates. Lactose Galactose Glucose- Substrate: Lactose Enzyme: Lactase 2 1 Enzyme-substrate complex The bond is broken between glucose and galactose 3 The substrate, lactose, binds to the enzyme forming an enzyme- substrate complexarrow_forward
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