Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 6.5, Problem 1SB
Summary Introduction
To review:
The reason for an enzyme-catalyzed reaction reaching a saturation level when the substrate concentration is increased.
Introduction:
Enzymes are the protein
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Explain 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.
Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations.
Why do we not determine the initial reaction rate when the enzyme is saturated with substrate?
Chapter 6 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 6.1 - Prob. 1SBCh. 6.1 - In thermodynamics, what is meant by an isolated...Ch. 6.2 - Prob. 1SBCh. 6.2 - Prob. 2SBCh. 6.2 - Distinguish between exergonic and endergonic...Ch. 6.3 - Prob. 1SBCh. 6.3 - How are coupled reactions important to cell...Ch. 6.4 - How do enzymes increase the rates of the reaction...Ch. 6.4 - Can enzymes alter the G of a reaction?Ch. 6.5 - Prob. 1SB
Ch. 6.5 - What is the difference between competitive and...Ch. 6.5 - Prob. 3SBCh. 6.6 - Prob. 1SBCh. 6 - The capacity to do work best defines: a metabolic...Ch. 6 - The assembly of proteins from amino acids is best...Ch. 6 - When two glucose molecules react to form maltose:...Ch. 6 - When glucose reacts with ATP to form...Ch. 6 - In the following graph: A represents the product....Ch. 6 - Which of the following methods is not used by...Ch. 6 - In an enzymatic reaction: a. the enzyme leaves the...Ch. 6 - Which of the following statements about the...Ch. 6 - Which of the following statements about inhibition...Ch. 6 - Which of the following statements is incorrect? a....Ch. 6 - Prob. 11TYKCh. 6 - Discuss Concepts Trace the flow of energy through...Ch. 6 - Prob. 13TYKCh. 6 - Prob. 14TYKCh. 6 - Prob. 15TYKCh. 6 - Prob. 16TYKCh. 6 - Prob. 17TYKCh. 6 - Prob. 1ITDCh. 6 - Prob. 2ITDCh. 6 - Prob. 3ITD
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- In an enzyme-catalyzed reversible reaction what happens when a) rate of change of enzyme-substrate complex concentration with time is positive b) rate of change of enzyme-substrate complex concentration with time is zero 9:0arrow_forwardHow does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?arrow_forwardWhat is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?arrow_forward
- What are the rate constants for the enzyme-catalyzed reaction?arrow_forwardAspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.arrow_forwardWhat is the difference between Vo and Vmax? Why do enzyme-catalyzed reactions show substrate saturation? What are the units of enzyme activity?arrow_forward
- Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.arrow_forwardDescribe the rate of enzyme-catalyzed reaction with increasing substrate concentration at constant enzyme concentration. In what ways does hydrogen ion concentration affect enzyme activity?arrow_forwardThe value of Vmax for an enzyme-catalyzed reaction: A) most often reflects the chemical steps of catalysis B) can be determined from initial velocities that are linear with respect to substrate concentration OC) is limited only by the amount of substrate supplied D) can be converted to kcat/Km by accounting for the enzyme concentration OE) is higher for enzymes that also exhibit higher Km valuesarrow_forward
- Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µMarrow_forwardYou have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!arrow_forwardMany isolated enzymes, if incubated at 37°C, will be denatured. However, if the enzymes are incubated at 37°C in the presence of substrate, the enzymes are catalytically active. Explain this apparent paradox.arrow_forward
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