Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 5TYU
Explain the lock-and-key model of enzyme activity. What is incorrect about this model?
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Define the word "enzyme inhibition."
Describe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
Chapter 8 Solutions
Biological Science (7th Edition)
Ch. 8 - 2. What is a transition state?
a. the shape...Ch. 8 - 3. How does pH affect enzyme-catalyzed...Ch. 8 - Explain how feedback inhibition regulates...Ch. 8 - 5. Explain the lock-and-key model of enzyme...Ch. 8 - If you were to expose glucose to oxygen on your...Ch. 8 - Using what you have learned about changes in Gibbs...Ch. 8 - Prob. 10TYPSSCh. 8 - 15. The functional form of PAH contains four...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of inhibitor you identified it as. If you were to add 5nM of a reversible inhibitor, the Km for the measured enzyme catalyzed reaction would ______ (Increase, Decrease, Stay the same) to ______µM (choose appropriate value) and Vmax would _______ (Increase, Decrease, Stay the same) to ______µMs-1. So, this inhibitor is a ______ (Competitive, Uncompetitive, Mixed) inhibitor. Conditions: kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µMarrow_forwardDescribe the induced-fit model of enzyme activity. *arrow_forwardExplain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.arrow_forward
- What type of enzyme regulation is the most readily (quickly) reversible?arrow_forwardIn the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1arrow_forwardWhy must enzyme activity be monitored under standard conditions?arrow_forward
- What is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?arrow_forwardBy using Excel or GoogleSheets, graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and V values for the inhibited and uninhibited reactions? Is the inhibitor competitive or max noncompetitive? [S] (mM) V, No Inhibitor (mmol min-') V, Inhibitor Present (mmol min-') 1× 10-4 5 × 10-4 1.5 × 10-3 2.5 × 10-3 5 × 10-3 0.026 0.092 0.136 0.150 0.010 0.040 0.086 0.120 0.165 0.142 Activatearrow_forwardPlease handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License