4. The following rate constants have been determined for a Michaelis –Menen enzyme: ki = 2.5 x 10$ M' s', k.1 =2 x 10³ s', and k2= 5 x 10ª s'. a. Calculate Ks and Km for this enzyme. b. Does the substrate binding approach equilibrium or the steady state? Explain why.
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.
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![4. The following rate constants have been determined for a Michaelis -Mena enzyme: kı = 2.5 x
10$ M' s', k.1 = 2 x 103 s!, and k2= 5 x 10* s'.
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a. Calculate K, and Km for this enzyme.
b. Does the substrate binding approach equilibrium or the steady state? Explain why.
c. In a 500ul reaction containing 2pmol of the enzyme and saturating levels of substrate.
What is the Vmax for the enzyme? Assume two active sites per enzyme molecule.
d. What substrate concentration would be needed for the reaction in 4c to achieve half
maximal velocity? Justify your answer mathematically.
e. What is the efficiency of this enzyme? Would this enzyme be considered a perfect
enzyme? Explain.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F5036d140-2c11-452f-a064-2e477c031fc5%2F2d2ccfde-3ccb-4144-b7a7-639c6d9237f8%2Fvomaay6_processed.jpeg&w=3840&q=75)
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