10. Applying the Michaelis-Menten Equation III A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction HAPPY = SAD. The researchers begin to characterize the enzyme. a. In the first experiment, with [E] at 4 nm, they find that the Vmax is 1.6 µM s. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b. In the second experiment, with [E:] at 1 nm and [HAPPY] at 30 µM, the researchers find that Vo = 300 nMs. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c. 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 are repeated, the measured Vmax in -1 (a) is increased to 4.8 µM s*, and the measured Km in (b) is now 15 µm. Calculate the values of a and a' for ANGER. d. Based on the information given, what type of inhibitor is ANGER?
10. Applying the Michaelis-Menten Equation III A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction HAPPY = SAD. The researchers begin to characterize the enzyme. a. In the first experiment, with [E] at 4 nm, they find that the Vmax is 1.6 µM s. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b. In the second experiment, with [E:] at 1 nm and [HAPPY] at 30 µM, the researchers find that Vo = 300 nMs. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c. 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 are repeated, the measured Vmax in -1 (a) is increased to 4.8 µM s*, and the measured Km in (b) is now 15 µm. Calculate the values of a and a' for ANGER. d. Based on the information given, what type of inhibitor is ANGER?
Chemistry
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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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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
![10. Applying the Michaelis-Menten Equation III A research group discovers a
new version of happyase, which they call happyase*, that catalyzes the chemical
reaction HAPPY = SAD. The researchers begin to characterize the enzyme.
a. In the first experiment, with [E:] at 4 nm, they find that the Vmax is
1.6 µM s1. Based on this experiment, what is the kcat for happyase*?
(Include appropriate units.)
b. In the second experiment, with [E:] at 1 nm and [HAPPY] at 30 µM, the
researchers find that Vo = 300 nMs. What is the measured Km of
S
%3D
happyase* for its substrate HAPPY? (Include appropriate units.)
c. 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 are repeated, the measured Vmax in
(a) is increased to 4.8 µM s, and the measured Km in (b) is now 15 µM.
Calculate the values of a and a' for ANGER.
d. Based on the information given, what type of inhibitor is ANGER?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fbad36464-4e5e-43b7-921a-6395099007d8%2Ff55312c4-f112-4208-8623-aeeee752c166%2Fq58069f_processed.png&w=3840&q=75)
Transcribed Image Text:10. Applying the Michaelis-Menten Equation III A research group discovers a
new version of happyase, which they call happyase*, that catalyzes the chemical
reaction HAPPY = SAD. The researchers begin to characterize the enzyme.
a. In the first experiment, with [E:] at 4 nm, they find that the Vmax is
1.6 µM s1. Based on this experiment, what is the kcat for happyase*?
(Include appropriate units.)
b. In the second experiment, with [E:] at 1 nm and [HAPPY] at 30 µM, the
researchers find that Vo = 300 nMs. What is the measured Km of
S
%3D
happyase* for its substrate HAPPY? (Include appropriate units.)
c. 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 are repeated, the measured Vmax in
(a) is increased to 4.8 µM s, and the measured Km in (b) is now 15 µM.
Calculate the values of a and a' for ANGER.
d. Based on the information given, what type of inhibitor is ANGER?
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