EBK CAMPBELL BIOLOGY
10th Edition
ISBN: 9780136539414
Author: Reece
Publisher: VST
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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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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
Is the dependent variable the reaction time? And what is the controlled variables in this experiment and are there any controls that are used in this experiment?
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lock and key hypothesis is outdated!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?
Chapter 8 Solutions
EBK CAMPBELL BIOLOGY
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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- 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…arrow_forward1arrow_forwardGenetic 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_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
- i submitted this 3 times in bartleby and everyone gave differnt answers please answer correctlyarrow_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_forward(e) Write 3 assumptions that could be made when using the type of support materials as suggested in (d).arrow_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_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_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License