Based on the experiment described below determine the Michaelis constant of the enzyme involved to two decimal places. Include any appropriate units. In your working out do not round intermediate results and only round the final value as required. A student in studied the kinetics of acid phosphatase. Acid phosphatase hydrolyses p-nitrophenyl phosphate into phosphate and p-nitrophenol. Reactions contains 250 microlitres p-nitrophenyl phosphate, 50 microlitres 0.1mg.ml/-1 acid phosphatase and 200 microlitres 100mM citrate buffer pH 4.8 They measured the initial rate of enzyme activity (nmol p-nitrophenol produced/min) for different concentrations of p-nitrophenyl phosphate (mmol/L) included in the reaction. The collected data was transformer, a Lineweaver Burk plot, similar to the general one depicted below, was created and the straight-line equation generated from the fitted data.
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.
Based on the experiment described below determine the Michaelis constant of the enzyme involved to two decimal places. Include any appropriate units. In your working out do not round intermediate results and only round the final value as required.
A student in studied the kinetics of acid phosphatase. Acid phosphatase hydrolyses p-nitrophenyl phosphate into phosphate and p-nitrophenol.
Reactions contains 250 microlitres p-nitrophenyl phosphate, 50 microlitres 0.1mg.ml/-1 acid phosphatase and 200 microlitres 100mM citrate buffer pH 4.8
They measured the initial rate of enzyme activity (nmol p-nitrophenol produced/min) for different concentrations of p-nitrophenyl phosphate (mmol/L) included in the reaction. The collected data was transformer, a Lineweaver Burk plot, similar to the general one depicted below, was created and the straight-line equation generated from the fitted data.
![1/ Enzyme activity (min/nmol)
1/Vo = 3.0651x 1/[S] + 0.6573
1/ substrate concentration (L/mmol)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F49aa25b9-2c60-42bd-8193-402bb4db0498%2F497cb8be-dfeb-4503-9a37-cb0d83be77b1%2Fdtcehrx_processed.png&w=3840&q=75)
Step by step
Solved in 4 steps with 5 images
