2. You measured the initial velocity of an enzyme in the absence of inhibitor and with inhibitor A or inhibitor B. In each case the inhibitor is present at 10 microMolar. The data are shown in the following table. a. Determine Km and Vmax of the enzyme. b. Determine the type of inhibition imposed by inhibitor A. C. Determine the type of inhibition imposed by inhibitor B. [S], mM 0.333 0.40 0.50 0.666 1.0 2.0 Velocity, (M s ¹) x 10² Uninhibited 1.65 1.86 2.13 2.49 2.99 3.72 Velocity, (M s ¹) x 107 Inhibitor A 1.05 1.21 1.43 1.74 2.22 3.08 Velocity, (M s¹) x 107 Inhibitor B 0.794 0.893 1.02 1.19 1.43 1.79
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.
PLEASE READ (CORRECTION):
b.) Determine the type of inhibition imposed by inhibitor A and calculate Ki
c.) Determine the type of inhibition imposed by inhibitor B and calculate Ki
Trending now
This is a popular solution!
Step by step
Solved in 2 steps with 3 images