1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 им. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and K, for the enzyme. c. [S] (mM) (1) V. (2) V- (3) V- [(umol/(ml.s)] [(umol/(ml.s)] [(umol/(ml.s)] 2 7.6 4.4 6.6 14.6 8.6 11.4 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
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.
Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
µM.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and KM for the enzyme.
![1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
им.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and K, for the enzyme.
c.
[S] (mM)
(1) V.
(2) V-
(3) V-
[(umol/(ml.s)]
[(umol/(ml.s)]
[(umol/(ml.s)]
2
7.6
4.4
6.6
14.6
8.6
11.4
26.6
16.4
17.8
16
45.8
29.8
24.6
24
60
40.8
28.2](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0d2cb750-34ee-4640-acc6-437307e7a6b1%2F8723e9dd-5afa-4c05-aab1-6681075fe937%2Fkhmf5pg.jpeg&w=3840&q=75)
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