CAMPBELL BIOLOGY MOD MASTERING (18 WEEK)
12th Edition
ISBN: 9780136920335
Author: Urry
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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Step 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).
Practice
Mira Gendy
1 of 1
Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written
out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable.
II
Substrate Concentration [S]
The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme.
Connect the primary structure of the enzyme to its overall shape.
I U
x X2 5
Initial Rate of Reaction
ENZYME CATALYSIS lab
Construct a hypothesis addressing the effect concentration will have on rate of reaction.
What chemical reaction is being catalyzed in the experiment? Label the substrate(s), enzyme and product(s).
Chapter 8 Solutions
CAMPBELL BIOLOGY MOD MASTERING (18 WEEK)
Ch. 8.1 - Prob. 1CCCh. 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 - Prob. 3CCCh. 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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- A researcher has developed an assay to measure the activity of an important enzyme present in pancreatic 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.arrow_forward6X9 X What are the steps for an enzyme to create a product in order: 1. The energy of activation is lowered so the reaction can happen quicker. 2. Substrate attaches to the active site. 3. The product is created and released from the active site. 4. The energy of activation is lowered so the reaction can happen slower. 5. A specific substrate attaches to the active site. Selected Answer: Answers: 5 -- 4 --> 3 5--1--> 3 2 1 -> 3 5 -- 4 --> 3 2--> 4 --> 3arrow_forwardC)|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?arrow_forward
- Determine how reaction rate (velocity) varies with substrate concentration. F3 $ 4 Substrate concentration R F Additional substrate is added when substrate concentration is low. F4 % 5 T Rate increases G 6 HOLL F5 & H 7 F6 YU J *00 8 DELL F7 K ( 9 Substrate is added when enzyme is saturated with substrate. F8 Rate decreases O Answer Bank F9 P W F10 { [ + 11 F11 } 1 F12 Additional substrate is added when substrate concentration is high but is not yet saturating. Backspace Rate is unchanged Enter Insert Print Screen Delete Home Scroll Lock End 8:26 PM 2 10/15/2023 + PgUp Pause Break PgDnarrow_forwardFill 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…arrow_forwardENZYME CATALYSIS lab Construct a hypothesis addressing the effect concentration will have on rate of reaction.arrow_forward
- A 45 year-old male presents with fever and cough. He is found to have bacterial pneumonia. He is administered a drug that inhibits bacterial enzyme that catalyzes bacterial DNA synthesis. The drug cited above produced the kinetic data shown below. The mechanism of action of the drug is non-competitive inhibition of enzyme; drug binds to active site. Please explain.arrow_forwardAn enzyme with a Km of 3 X 10-4 M was tested at an initial substrate concentration of 10-5 M. In 1 minute, 5% of the substrate was found to be utilized. (a) What percentage of the substrate was utilized in 5 minutes? (b) If the initial substrate concentration had been 8 X 10-7 M, what percentage of the substrate would have been utilized in 5 minutes? (c) Vmax =? (d) How long would it take to utilize 50% of the substrate at 8 X 10-7 M? (e) How long would it take to utilize 75% of the substrate at 10-5 M?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_forward
- Consider 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_forwardBriefly describe 1 way which enzyme activity can be regulated in the cell. How do the kinetics of a regulatory enzyme differ from a non-regulated enzyme?arrow_forwardsubstrate active site enzyme enzyme + substrate entering active site FIGURE 5 enzyme changes shape slightly as substrate enters active site, making the fit more precise enzyme/substrate complex Lock : Key enzyme/products complex products 5 enzyme + products leaving active site 5. Looking at Figure 5 above, how is the enzyme similar to a lock and a key? 6. Complete the following analogy using the terms show in figure 5 (Enzyme and Substrate). 7. If the substrate in the first image in the left of the series is a disaccharide such as sucrose, what is the enzyme doing to the disaccharide? 8. The picture above is showing what is known in biochemistry as the "lock and key theory." Explain why you think this theory is used to describe enzymes.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License