Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 8, Problem 9TYU
Summary Introduction
To propose: A model on the basis of graph to explain the molecular event occurring at each stage of the reaction profile.
Concept introduction: Enzymes are catalysts that enhance the rate of a reaction. The enzyme assay is a technique performed in laboratories to determine the concentration and activity of an enzyme. It is a very useful technique as it can provide information about the interaction of the enzyme with the substrate, drugs, inhibitors, and others.
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Enzyme Investigation An enzyme was isolated from digestive juices taken from the small intestine. An experiment was set up to test the ability of the enzyme to break down protein. Two test tubes, labeled A and B, were placed in a hot water bath at 37°C, human body temperature. Test tube A contained only protein and test tube B contained protein and the enzyme. The chart below shows the set-up. After two hours, the contents of both test tubes were analyzed. Test tube A showed only the presence of protein. Test tube B showed the presence of the end products of protein digestion, indicating the enzyme had successfully broken down the protein. Identify the end products of protein digestion that made up the contents of test tube B after the two hours.
C)|Myth: The specificity of an enzyme for its substrate is explained by the lock and key hypothesis. Fact: The
lock and key hypothesis is outdated! What is our current model for understanding regarding how enzymes
recognize and bind to substrates?
Fill the blank with the option below
The substrate concentration at which an enzyme-catalyzed reaction proceeds at on-half its maximum velocity
The rate enhancement of the enzyme catalyzed reaction over uncatalyzed reaction
The rate of the reaction when the concentration of the products is zero and the reverse rate is negligible
The rate at which the enzyme-substrate complex is formed
The number of time an enzyme molecule transforms a substrate molecule per unit of time
The proportionality constant that relates the velocity of a chemical reaction to the concentrations of the reactants
The maximum velocity of an enzymatic reaction when the binding site is saturate with substrate
A measure of the catalytic activity of an enzyme at low concentrations of substrate
The rate constant for the equilibrium between the reactants and the enzyme-substrate complex
1. Vo
2.
4.
3. V₁
Acronym Parameter
6.
7.
I
5. Km
8.
1
I
9. AAG
10. AG
rate constant
rate of
disappearance
I
specificity
constant…
Chapter 8 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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- Genetic engineering of enzymes to be utilized for bioremediation efforts results in which of the following changes? (you may select more than one) Decrease in the concentration required to reach one half maximal velocity. Increase in hydrogen bonding between substrate and enzyme. Primary sequence alterations resulting in 3D structural changes in the substrate binding site. Decrease in the maximum activity the enzyme can achieve in ideal conditions.arrow_forwardExamine the figure below, which compares the energetics of a catalyzed and uncatalyzed reaction during the progress of the reaction from substrate (S) to product (P). The highest peak in such a diagram corresponds to the transition state, which is an unstable, high-energy arrangement of substrate atoms that is intermediate between substrate and product. The free energy required to surmount this barrier to the reaction is termed the activation energy. Enzymes function by lowering the activation energy, thereby allowing a more rapid approach to equilibrium. UNCATALYZED activation energy progress of reaction CATALYZED activation energy S ES | progress of reaction free energy free energyarrow_forwardi submitted this 3 times in bartleby and everyone gave differnt answers please answer correctlyarrow_forward
- A dichotomous key works by determining positive and negative reactions to different biochemicals. Why does this method allow us to identify one species of organism from another? – for this question, do not describe the dichotomous key procedure, think about why it works, what are biochemical reactions based on? Think enzymatic pathways, what are enzymes, what are they a reflection of? Keep the answer between 2-3 sentencesarrow_forward1. Carols first question was, “What is an enzyme” a. Use the enzyme lactase as an example, and explain how it functions(figure 4.1) b. What is the substrate for lactase. c. What are the end products of this reaction?arrow_forwardPlease answerarrow_forward
- Q1: Why is it important that enzymes are not permanently altered when they bind with substrate molecules? Q2: How would a higher temperature or higher salt concentration make it more difficult for an enzyme to function effectively? Q3: If a cell was unable to produce a particular enzyme necessary for a metabolic pathway, describe how the absence of that enzyme would affect the cell.arrow_forward| 2 3 I 4 I 5 I 6 I 7 Directions: Graph the data (line graph); label both axes. DATA TABLE 1 Temperature (°C) Enzyme Activity 10 10 20 15 30 25 40 45 50 35 60 20 Temperature (C) 1. According to the graph, what is the best (optimum) temperature for enzyme activity? Explain your reasoning. 2. What happens to the enzyme above the optimum temperature? 26°F F12 PrtSc Insert Delete F7 FO F9 Backspac 7 8. R P G K 近arrow_forwardAn enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asparrow_forward
- Competitive inhibitors have been developed as pharmaceuticals are not naturally occurring must be identical in shape and charge to the enzyme's natural substrate prevent the enzyme from binding its natural target even in the presence of an excess of that natural targetarrow_forwardTo examine: Whether the statement, "An enzyme reaches a maximum rate at high substrate concentration because it has a fixed number of active sites where substrate binds", is true or false.arrow_forwardWhich of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are truearrow_forward
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