

1. An enzyme with a Km of 1x10 % M was assayed using an initial substrate...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
An enzyme that follows Michaelis-Menten kinetics has a initial velocity of 300 nM/s at a substrate concentration of 30 uM. The maximum velocity of 400 nM/sec. What is the Km for this enzyme in uM? (Give your answer as a number only. Type your response
An enzyme that follows Michaelis-Menten kinetics has a KM value of 20.0 μM and a kcat value of 211 s−1. At an initial enzyme concentration of 0.0100 μM, the initial reaction velocity was found to be 1.07×10−6 μM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures.
3. Acid Phosphatase was assayed at [S] = 2x10-5 M. The Km for the substrate was 5x10-4 M. At the end of one minute 2.5% of the substrate, pNPP, had been converted to pNP (a product). Answer the following questions using this information: a) What percent of PNPP will be converted at the end of 3.5 minutes assuming product formation is in 1 st order of reaction? (3 points) b) What will be the product concentration at the end of...
Acid Phosphatase was assayed at [S] = 2x10-5 M. The Km for the substrate was 5x10-4 M. At the end of one minute 2.5% of the substrate, PNPP, had been converted to PNP (a product). Answer the following questions using this information: a) What percent of PNPP will be converted at the end of 3.5 minutes assuming product formation is in 1 st order of reaction? (3 points) b) What will be the product concentration at the end of 3.5...
3. Acid Phosphatase was assayed at [S] =2x10-5 M. The Km for the substrate was 5x10-4 M. At the end of one minute 2.5% of the substrate, PNPP, had been converted to pNP (a product). Answer the following questions using this information: a) What percent of PNPP will be converted at the end of 3.5 minutes assuming product formation is in 1st order of reaction? (3 points) b) What will be the product concentration at the end of 3.5 minutes?...
7. a) In an enzyme catalyzed reaction which follows the Michaelis-Menten kinetics. The substrate concentration (Km, Michaelis constant) needed to reach 50% of the maximum reaction velocity (Vmax) is 20 μΜ. What substrate concentration is required to obtain at least 75% of the maximum reaction velocity? Show the work to get full points. (5 points) b) You want to load 10 μg of protein in 15 μL into one of the 10% polyacrylamide gel well. The protein needs to be...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
Assuming that an enzyme catalyzed reaction follows Michaelis-Menten kinetics with a Km of 1 x 10-6 M. If the initial reaction rate (V0) is 0.1 μmol/min at 0.1 M, what would it be at 0.01 M, 10-3M, and 10-6 M?
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM