Campbell Biology in Focus, Books a la Carte Edition; Modified Mastering Biology with Pearson eText - ValuePack Access Card - for Campbell Biology in Focus (2nd Edition)
2nd Edition
ISBN: 9780134433769
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman
Publisher: PEARSON
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Chapter 6, Problem 8TYU
SCIENTIFIC INQUIRY
DRAW IT A researcher has developed an assay to measure the activity of an important enzyme present in liver cells growing in culture. She adds the enzyme’s substrate to a dish of cells and then measures the appearance of reaction products. The results are graphed as the amount of product on the y-axis versus time on the x-axis. The researcher notes four sections of the graph. For a short period of time, no products appear (section A). Then (section B) the reaction rate is quite high (the slope of the line is steep). Next, the reaction gradually slows down (section C). Finally, the graph line becomes flat (section D). Draw and label the graph, and propose a model to explain the molecular events occurring at each stage of this reaction profile.
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You design an experiment to explore the effects of enzyme concentration on the rate of glucose (product) production. In the experiment, you prepare 5 tubes with equal amounts of water and substrate but altered the amount of enzyme. Tube #1 did not have enzyme, Tube #2 had 100 mg of enzyme, Tube #3 had 200 mg of enzyme, Tube #4 had 300 mg of enzyme, Tube #5 had 400 mg of enzyme. The results are summarized in the graph.
Select all that apply.
Given enough time all tubes (#1-5) would reach 1100 mg/dL.
The substrate in tube #1 was denatured at 40 minutes.
The fastest rate of reaction was in Tube #4.
Adding more enzyme to Tube #5 at 40 minutes would produce more product.
Tube #4 and #5 have run out of substrate at 40 minutes.
In a highly high-temperature environment, you placed an enzyme and some substrates. You've seen that there hasn't been any reaction. Applying what you have learned on enzyme activity, how would you explain what occurred?
A. The enzyme was not placed at a pH level that would allow it to react at its maximum rate.
B. There are not enough enzymes for the reaction to occur.
C. The enzyme may have denatured or broken down due to the high temperature of the environment, resulting in no reaction.
D. There are not enough substrates for reaction to occur.
Substrate concentration affects enzyme activity. Determine what would occur when there are too many substrates and fewer enzymes?
A. No enzyme activity would occur.
B. The reaction rate would continuously increase.
C. The reaction would speed up tremendously.
D. Maximal rate of reaction would occur.
Enzyme activity mainly involves the active site and the substrate. How would you compare the active site from the substrate?
A. The substrate…
cells can regulate different processes in two ways. they can turn on and off the genes that make enzymes, or they can:
A. decrease the amount of energy needed to carry out the preferred process
B. increase the activation energy of a reaction
C. regulate the enzymes that are already made
D. increase the amount of energy needed to carry out the preferred process
Chapter 6 Solutions
Campbell Biology in Focus, Books a la Carte Edition; Modified Mastering Biology with Pearson eText - ValuePack Access Card - for Campbell Biology in Focus (2nd Edition)
Ch. 6.1 - MAKE CONNECTIONS How does the second law of...Ch. 6.1 - Describe the forms of energy found in an apple as...Ch. 6.2 - Cellular respiration uses glucose and oxygen,...Ch. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.3 - How does ATP typically transfer energy from...Ch. 6.3 - Prob. 2CCCh. 6.3 - MAKE CONNECTIONS Does Figure 6.10a show passive or...Ch. 6.4 - Many spontaneous reactions occur very slowly. Why...Ch. 6.4 - Why do enzymes act only on very specific...
Ch. 6.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 6.5 - How do an activator and an inhibitor have...Ch. 6 - Choose the pair of terms that correctly completes...Ch. 6 - Prob. 2TYUCh. 6 - Which of the following metabolic processes can...Ch. 6 - If an enzyme in solution is saturated with...Ch. 6 - Some bacteria are metabolically active in hot...Ch. 6 - If an enzyme is added to a solution where its...Ch. 6 - DRAW IT Using a series of arrows, draw the...Ch. 6 - SCIENTIFIC INQUIRY DRAW IT A researcher has...Ch. 6 - SCIENCE, TECHNOLOGY, AND SOCIETY Organophosphates...Ch. 6 - FOCUS ON EVOLUTION A recent revival of the...Ch. 6 - FOCUS ON ENERGY AND MATTER Life requires energy....Ch. 6 - SYNTHESIZE YOUR KNOWLEDGE Explain what is...
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- The diagram shows the mechanism of a general enzyme‑catalyzed reaction. Put the labels in the correct locations. The abbreviations E, P and S indicate the enzyme, product, and substrate, respectively.arrow_forwardStep 1: Depict E + S • Draw an enzyme and one substrate. Show and label the substrate binding site on the enzyme. Step 2: Depict ES • Draw the enzyme bound to the substrate in the substrate binding site. Step 3: Depict EP • Draw the enzyme bound to the product (the changed substrate). Step 4: Depict E + P • Draw the enzyme with the product released. (Note: the enzyme is returned to its original state and can be reused.) Step 5: Impact of Inhibitors • Go to the prompts that have arrows pointing to the E + S picture you drew and fill in the blanks with the appropriate type of inhibitor (competitive or non-competitive/allosteric).arrow_forwardThe image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.arrow_forward
- Refer to image below and answer the following: 1. What is the optimum temperature (degrees celsius) for the enzyme activity? 2. At what temperature when the emzyme was totally denatured?arrow_forwardConsider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?arrow_forwardA technician investigated the effect of temperature on the rate of an enzyme- controlled reaction. At each temperature, she started the reaction using the same concentration of substrate. 15 amount of 37 C product in 11. Give one other factors the technician would have controlled. 10 60 "C 12. Explain the difference in the initial rate of reaction at 60°C and 37°C. 13. Explain the difference in the rates of reaction at 60°C and 37°C between 20 and 10 20 30 Time after start of reaction i minutes 40 minutes.arrow_forward
- Examine the metabolic pathway shown in Figure 8.18. Draw a table indicating the relative concentrations of molecules A, B, C, and D if you were to remove Enzyme 1, 2, or 3 from the system.arrow_forwardWhich of the following describes a reaction that requires substrate 1 to bind the the enzyme, then substrate 2 binds, and then the products are produced? A. No ternary complex B. Ordered ternary complex C. Ping-Pong D. Random ternary complexarrow_forwardLeia wants to determine the effect of enzyme concentration on enzyme activity using potato samples and hydrogen peroxide. However, her results do not follow the theoretical trend and thus she can't draw any conclusions from the data obtained. What might have caused errors in the experiment? I. Placing potato samples under room temperature II. Different treatments, with potato being proportional to the volume of hydrogen peroxide III. Placed the same amount of hydrogen peroxide for a different amount of potatoes IV. Placed the same amount of potatoes for a different volume of hydrogen peroxidearrow_forward
- The purpose of this experiment is to determine how the activity of an enzyme can change under certain conditions: temperature, pH, substrate concentration Introduction Purpose statement is specific, complete and uses proper scientific vocabulary Hypothesis statement is clear, logical and scientifically sound Contains sufficient background information relevant to the lab Accurate use of examples and scientific terminology Clear, concise (max 1 page; single spaced) Step 1: Obtain a sample amount of a hard fruit or vegetable, such as an apple, cut it into smaller equal pieces, and measure on a digital scale of 10g. Step 2: Get 100ml of room temperature tap water and add it into a glass cup, heat it on a hot plate until reaches 37 Celsius Step 3: Add the apple sample into the glass cup with the tap water and mix gently. Let the mixture to sit for 5 minutes. Step 4: With a kitchen thermometer measure the temperature of the apple mixture. Step 5: In a glass cup add 3mL of 3% hydrogen…arrow_forwardIn one word, describe the function of enzymes. In one word, describe how enzymes affect the rate of biochemical reactions in our system.arrow_forwardExamine the graph showing the rate of reaction versus temperature for an enzyme–catalyzed reaction in a human. a. Describe what is happening to the enzyme at around 40°C. b. Explain why the line touches the x-axis at approximately 20°C and 45°C. c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License