A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
Chemistry & Chemical Reactivity
10th Edition
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions
Section14.7: Reaction Mechanisms
Problem 1.2ACP
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Concept explainers
Catalysis and Enzymatic Reactions
Catalysis is the kind of chemical reaction in which the rate (speed) of a reaction is enhanced by the catalyst which is not consumed during the process of reaction and afterward it is removed when the catalyst is not used to make up the impurity in the product. The enzymatic reaction is the reaction that is catalyzed via enzymes.
Lock And Key Model
The lock-and-key model is used to describe the catalytic enzyme activity, based on the interaction between enzyme and substrate. This model considers the lock as an enzyme and the key as a substrate to explain this model. The concept of how a unique distinct key only can have the access to open a particular lock resembles how the specific substrate can only fit into the particular active site of the enzyme. This is significant in understanding the intermolecular interaction between proteins and plays a vital role in drug interaction.
Question
![A research group discovers a neW version oI happyasee, which they
nappyase", that catalyzes the chemical reaction
HAPPY = SAD
The researchers begin to characterize the enzyme.
In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat
for happyase*?
kcat
400
S
In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i
the measured Km of happyase* for its substrate HAPPY?
Km
10 x10–6
Incorrect
Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a
reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two
experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM.
S
For the inhibitor ANGER, calculate the values of a' and a.
a'
2
Incorrect
2](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8b43fcf2-0c31-4621-bb6f-bb4e7d883fd1%2F38e34432-b1de-42b7-be0c-8507960b9415%2F6bcx7n.png&w=3840&q=75)
Transcribed Image Text:A research group discovers a neW version oI happyasee, which they
nappyase", that catalyzes the chemical reaction
HAPPY = SAD
The researchers begin to characterize the enzyme.
In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat
for happyase*?
kcat
400
S
In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i
the measured Km of happyase* for its substrate HAPPY?
Km
10 x10–6
Incorrect
Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a
reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two
experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM.
S
For the inhibitor ANGER, calculate the values of a' and a.
a'
2
Incorrect
2
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