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Biochemistry
Rank from highest enzyme efficiency to lowest enzyme efficiency.

Rank from highest enzyme efficiency to lowest enzyme efficiency.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Rank from highest enzyme efficiency to lowest enzyme efficiency. To rank items as equivalent, overlap them.

## Enzyme Kinetics of β-lactam Antibiotics All of the kinetics work you performed in Parts F through P has allowed you to determine the values of k<sub>cat</sub> and K<sub>M</sub> of your enzyme for the substrate amoxicillin. You repeat all of these experiments with a series of additional β-lactam substrates, hoping to determine which of the β-lactams are more or less susceptible to hydrolysis by this newly discovered β-lactamase enzyme. ### Table: Kinetics Parameters for Various Antibiotics | Antibiotic | k<sub>cat</sub> (s⁻¹) | K<sub>M</sub> (µM) | |--------------|------------------|----------------| | Amoxicillin | 7 | 130 | | Cephalothin | 1,000 | 6,000 | | Cefotaxime | 14 | 7,900 | | Ceftazidime | 2.5 | 20,000 | | Aztreonam | 3.5 | 5,000 | | Imipenem | 0.09 | 2.9 | ### Explanation - **k<sub>cat</sub> (s⁻¹)**: The turnover number, or the number of substrate molecules converted to product per enzyme molecule per second. - **K<sub>M</sub> (µM)**: The Michaelis constant, indicative of the substrate concentration at which the reaction velocity is half of the maximum velocity (V<sub>max</sub>). These values provide insights into the efficiency of the enzyme in hydrolyzing each antibiotic. Lower K<sub>M</sub> values indicate higher affinity between enzyme and substrate, while higher k<sub>cat</sub> values suggest faster catalysis. ### Citation *Data based on published data for GES-14 in Table 2 from Delbrück H, Bogaerts P, Kupper MB, Rezende de Castro R, Bennink S, Glupczynski Y, Galleni M, Hoffmann KM, Bebrone C. Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases. Antimicrob Agents Chemother. 201
Transcribed Image Text:## Enzyme Kinetics of β-lactam Antibiotics All of the kinetics work you performed in Parts F through P has allowed you to determine the values of k<sub>cat</sub> and K<sub>M</sub> of your enzyme for the substrate amoxicillin. You repeat all of these experiments with a series of additional β-lactam substrates, hoping to determine which of the β-lactams are more or less susceptible to hydrolysis by this newly discovered β-lactamase enzyme. ### Table: Kinetics Parameters for Various Antibiotics | Antibiotic | k<sub>cat</sub> (s⁻¹) | K<sub>M</sub> (µM) | |--------------|------------------|----------------| | Amoxicillin | 7 | 130 | | Cephalothin | 1,000 | 6,000 | | Cefotaxime | 14 | 7,900 | | Ceftazidime | 2.5 | 20,000 | | Aztreonam | 3.5 | 5,000 | | Imipenem | 0.09 | 2.9 | ### Explanation - **k<sub>cat</sub> (s⁻¹)**: The turnover number, or the number of substrate molecules converted to product per enzyme molecule per second. - **K<sub>M</sub> (µM)**: The Michaelis constant, indicative of the substrate concentration at which the reaction velocity is half of the maximum velocity (V<sub>max</sub>). These values provide insights into the efficiency of the enzyme in hydrolyzing each antibiotic. Lower K<sub>M</sub> values indicate higher affinity between enzyme and substrate, while higher k<sub>cat</sub> values suggest faster catalysis. ### Citation *Data based on published data for GES-14 in Table 2 from Delbrück H, Bogaerts P, Kupper MB, Rezende de Castro R, Bennink S, Glupczynski Y, Galleni M, Hoffmann KM, Bebrone C. Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases. Antimicrob Agents Chemother. 201
### Enzyme Efficiency Activity This interactive module allows you to drag and arrange various substrates to determine their order based on enzyme efficiency. The goal is to rank the displayed substrates from the highest to the lowest enzyme efficiency. #### Substrates to Rank: - Cephalothin - Amoxicillin - Aztreonam - Ceftazidime - Imipenem - Cefotaxime #### Instructions: - **Drag and drop** each substrate into the provided box. - Arrange them from left (Best substrate with **highest enzyme efficiency**) to right (Worst substrate with **lowest enzyme efficiency**). #### Options: - **Reset**: Clears all selections and allows you to start over. - **Help**: Provides additional instructions or hints. #### Additional Feature: - A checkbox labeled "The correct ranking cannot be determined." - Select this option if you believe that the correct ranking cannot be established based on the given information. This activity aids in understanding the concept of enzyme efficiency and helps in visualizing how various substrates may perform differently in enzymatic reactions.
Transcribed Image Text:### Enzyme Efficiency Activity This interactive module allows you to drag and arrange various substrates to determine their order based on enzyme efficiency. The goal is to rank the displayed substrates from the highest to the lowest enzyme efficiency. #### Substrates to Rank: - Cephalothin - Amoxicillin - Aztreonam - Ceftazidime - Imipenem - Cefotaxime #### Instructions: - **Drag and drop** each substrate into the provided box. - Arrange them from left (Best substrate with **highest enzyme efficiency**) to right (Worst substrate with **lowest enzyme efficiency**). #### Options: - **Reset**: Clears all selections and allows you to start over. - **Help**: Provides additional instructions or hints. #### Additional Feature: - A checkbox labeled "The correct ranking cannot be determined." - Select this option if you believe that the correct ranking cannot be established based on the given information. This activity aids in understanding the concept of enzyme efficiency and helps in visualizing how various substrates may perform differently in enzymatic reactions.
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