Rank from highest enzyme efficiency to lowest enzyme efficiency.
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
Related questions
Question
Rank from highest enzyme efficiency to lowest enzyme efficiency. To rank items as equivalent, overlap them.
![All of the kinetics work you performed in Parts F through P has allowed you to determine the values of kcat and KM of your enzyme for the substrate amoxicillin. You repeat all of these experiments with a series of additional ß-
lactam substrates, hoping to determine which of the B-lactams are more or less susceptible to hydrolysis by this newly discovered B-lactamase enzyme.
kicat
(s)
Км
(uM)
Antibiotic
Amoxicillin
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
"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
B-lactamases. Antimicrob Agents Chemother. 2012 Nov:56(11):5618.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8aed6818-5f78-4d04-b2be-4c401a7b5b20%2F7451810f-889a-46eb-89db-01dc16a36f37%2Fks2o1nw_processed.png&w=3840&q=75)
Transcribed Image Text:All of the kinetics work you performed in Parts F through P has allowed you to determine the values of kcat and KM of your enzyme for the substrate amoxicillin. You repeat all of these experiments with a series of additional ß-
lactam substrates, hoping to determine which of the B-lactams are more or less susceptible to hydrolysis by this newly discovered B-lactamase enzyme.
kicat
(s)
Км
(uM)
Antibiotic
Amoxicillin
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
"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
B-lactamases. Antimicrob Agents Chemother. 2012 Nov:56(11):5618.
![Reset
Help
cephalothin
amoxicillin
aztreonam
ceftazidime
imipenem
cefotaxime
Best substrate (highest enzyme efficiency)
Worst substrate (lowest enzyme efficiency)
O The correct ranking cannot be determined.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8aed6818-5f78-4d04-b2be-4c401a7b5b20%2F7451810f-889a-46eb-89db-01dc16a36f37%2Ff029pbe_processed.png&w=3840&q=75)
Transcribed Image Text:Reset
Help
cephalothin
amoxicillin
aztreonam
ceftazidime
imipenem
cefotaxime
Best substrate (highest enzyme efficiency)
Worst substrate (lowest enzyme efficiency)
O The correct ranking cannot be determined.
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