Biology
12th Edition
ISBN: 9780134813448
Author: Audesirk, Teresa, Gerald, Byers, Bruce E.
Publisher: Pearson,
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Chapter 6.5, Problem 2TC
Summary Introduction
To draw: An enzyme in metabolic pathway for the synthesis of glycogen.
Introduction: Enzymes are proteins that play a key role in the activation of reaction involved in the
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Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the
statements that are true.
Without
enzyme
With
enzyme
A+B
Time
AB
O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction
O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the
uncatalyzed reaction
O c. The enzyme stabilizes the transition state for the reaction
Od. The reaction is exergonic
е.
The reaction is now spontaneous due to the addition of enzyme
Released Energy
Please 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.
Consider the graphic representation shown below for the free energy change for the overall reaction of Fructose-6-phosphate and ATP to form the products Fructose-1,6-biphosphate and ADP in the presence (blue line)
or absence (red line) of enzyme. Match each of the arrows (labeled A, B, C, or D) indicated in the graph with an apropriate description by dragging the letters into their corresponding box.
C
D
reactants
Fructose-6-phosphate
+ ATP
A
products
Fructose-1,6-biphosphate
+ ADP
Progress of the Reaction
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D BAc
В
C
Energy of activation for the
forward reaction in the
absence of enzyme
Energy of activation for the
forward reaction
Energy of activation for the
reverse reaction in absence
AG for the reaction
the
presence of enzyme
of enzyme
Energy
Chapter 6 Solutions
Biology
Ch. 6.1 - Prob. 1TCCh. 6.1 - Energy Unleashed Much like a cars engine, the...Ch. 6.1 - define energy and work?Ch. 6.1 - define potential energy and kinetic energy and...Ch. 6.1 - State and explain the first and second laws of...Ch. 6.2 - Is glucose breakdown endergonic or exergonic? What...Ch. 6.2 - Prob. 1CSCCh. 6.2 - describe how energy is captured and released by...Ch. 6.2 - explain exergonic and endergonic reactions and...Ch. 6.2 - explain activation energy?
Ch. 6.3 - Prob. 1TCCh. 6.3 - In hope of reducing plastic waste, some towns and...Ch. 6.3 - name and describe two important energy-carrier...Ch. 6.3 - explain coupled reactions?Ch. 6.4 - Can an enzyme catalyst make an endergonic reaction...Ch. 6.4 - You may have seen the almost magical glow of...Ch. 6.4 - explain how catalysts reduce activation energy?Ch. 6.4 - explain how enzymes function as biological...Ch. 6.5 - Health Watch Lack of an Enzyme Leads to Lactose...Ch. 6.5 - describe how cells regulate the rate at which...Ch. 6.5 - explain how poisons, drugs, and environmental...Ch. 6.5 - Prob. 2TCCh. 6 - Which of the following is True? a. Enzymes...Ch. 6 - Prob. 2MCCh. 6 - Prob. 3MCCh. 6 - Prob. 4MCCh. 6 - Prob. 5MCCh. 6 - Prob. 1FIBCh. 6 - Prob. 2FIBCh. 6 - Prob. 3FIBCh. 6 - Prob. 4FIBCh. 6 - Prob. 5FIBCh. 6 - Prob. 6FIBCh. 6 - Prob. 1RQCh. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - While vacuuming, you show off by telling a friend...Ch. 6 - Refute the following: According to evolutionary...Ch. 6 - Can a bear use all the energy contained in the...
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- Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.arrow_forwardBelow is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the Vmax value for this reaction. Report your answer to four significant figures in units of uM/min.arrow_forwardConsider two enzymes catalyzing two reactions (A --> B --> C ) in a metabolic cascade with their properties summarized below: Keg (for reaction) Enzyme Reaction KM Kcat / KM 102 M-1s-1 108 M-1s-1 1 A --> B 1 1 mM 2 B --> C 10 10 mM Initial concentrations are [A] = 0.1 mM and [B] = [C] = 0 and both enzymes are present at concentrations of 1 mM. After waiting for 1 ms, the concentrations of A, B, and C are measured. How do you expect the concentrations to be ordered? O [B] > [A] > [C] O [C] > [B] > [A] O [A] > [B] > [C] O [A] > [C] > [B] [C] > [A] > [B]arrow_forward
- Graph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.arrow_forwardIn biological systems, enzymes are used to accelerate the rates of certain bio- logical reactions. Glucoamylase is an enzyme that aids in the conversion of starch to glucose (a sugar that cells use for energy). Experiments show that 1 pg mol of glucoamylase in a 4% starch solution results in a production rate of glucose of 0.6 ug mol/(mL)(min). Determine the production rate of glucose for this system in the units of Ib mol/(ft³)(day). Ibmol Answer: 0.0639 ft day True Falsearrow_forwardSuggest the possible class of enzyme (or name of enzyme) for each of the enzyme-catalyzed reactions below. Briefly explain your answer.arrow_forward
- By 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_forwardAn enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.arrow_forwardYou 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 phosphatasearrow_forward
- the kinetics of an enzyme were analyzed in the absence of inhibitors, as well as in the presence of inhibitor A and inhibitor B. Using the given data below, construct or calculate the following (make sure the label graphs with appropriate axes and equations, and circle final answers) plot 1[S] as abscissa and 1/v as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots Calculate the; Km of enzyme in the reaction without inhibitor Km of the enzyme in the reaction with inhibitor (A dnB) Vmax of the uninhibited reaction Vmax of the inhibited reaction (A and B) What kind of inhibitor (A and B) was added to the enzyme-catalyzed reaction? Explain in terms of changes in Km and Vmaxarrow_forwardA generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.arrow_forwardConsider the hypothetical enzyme-catalyzed reaction: R → P Given the kinetic data below, calculate the KM, in mM, of the hypothetical enzyme for substrate R.arrow_forward
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