Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 6.2, Problem 3CC
Summary Introduction
To analyze:
Thecomparison between the reaction velocity of enzyme A or B.
Introduction:
Enzymes are protein molecules that function to enhance the
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An enzyme has a KM = 10 mM and Vmax = 100 mmol/min. Identify the substrate concentration (in mM) in which the velocity will near Vmax when there is a 10-fold decrease in KM.
An enzyme that catalyzes the reaction X ⇌ Y is isolated from two bacterial species. The enzymes have the same Vmax but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, and enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X] = 1 μM. Which curve corresponds to which enzyme? Explain.
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each
substrate concentration.
[S] = 1.75 mM
MM-s-1
[S] = 7.50 mM
[S] = 11.0 mM
DO
mM-s
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Chapter 6 Solutions
Principles of Biology
Ch. 6.1 - Which do you think has more entropy, an NaCl...Ch. 6.1 - Prob. 1TYKCh. 6.1 - Prob. 2TYKCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.2 - Prob. 1TYKCh. 6.2 - An inhibitor raises the Km for an enzyme but has...Ch. 6.3 - Prob. 1CCCh. 6.3 - Prob. 1TYK
Ch. 6.3 - Prob. 2TYKCh. 6.3 - Prob. 3TYKCh. 6.4 - Prob. 1CCCh. 6.4 - Prob. 1BCCh. 6.4 - Prob. 1TYKCh. 6.4 - Prob. 2TYKCh. 6.4 - Prob. 2CCCh. 6.5 - Prob. 1TYKCh. 6.6 - During the citric acid cycle, what happens to...Ch. 6.7 - Prob. 1CCCh. 6.7 - Prob. 2CCCh. 6.7 - Prob. 3CCCh. 6.7 - Prob. 1TYKCh. 6.7 - Prob. 2TYKCh. 6.7 - Prob. 3TYKCh. 6.8 - Prob. 1CCCh. 6.8 - Prob. 1TYKCh. 6 - According to the second law of thermodynamics....Ch. 6 - Reactions that release free energy are exergonic....Ch. 6 - Prob. 3TYCh. 6 - Prob. 4TYCh. 6 - Prob. 5TYCh. 6 - Prob. 6TYCh. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Prob. 10TYCh. 6 - Describe the mechanism and purpose of feedback...Ch. 6 - What causes the rotation of the y subunit of ATP...Ch. 6 - PRINCIPLES A principle of biology is that living...Ch. 6 - Discuss how life can maintain its order in spite...Ch. 6 - Prob. 2CBQ
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- You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the Km to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? 0.09 MS-1 O 0.133 Ms-1 O 0.18 Ms ¹ 9 Ms-1 O 0.018 Ms-1 0.2 MS-1arrow_forwardAn 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_forwardAn enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?arrow_forward
- An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.arrow_forwardAn enzyme catalyzes the reaction A --> B. The enzyme is present at a concentration of 2 nM, and the Vmax is 10 uM/s. The Km for substrate A is 10mM Calculate the initial velocity of the reaction, Vo, when the substrate concentration is a)2 mM and b) 30 mM.arrow_forwardYou are attempting to determine KM by measuring the reaction velocity at different substrate concentrations, but you do not realize that the substrate tends to precipitate under the experimental conditions you have chosen. How would this affect your measurement of KM?arrow_forward
- Solve the Michaelis-Menten equation for KM when vo=Vmax/2. What does this tell you about the relationship between substrate concentration and enzymes with high KM values? With low KM values?arrow_forwardThe typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURKarrow_forwardAn enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.arrow_forward
- A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)arrow_forwardAn enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.arrow_forwardAn 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.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License