8L.16.2 Part AAn enzyme that follows Michaelis-Menten kinetics has a KM value of 11.0 µM and a keat value of 151 s-¹. At an initial enzyme concentration of 0.0100 μM, theinitial 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.► View Available Hint(s)[S] =SubmitIV—| ΑΣΦ/VE?μΜ

An enzyme is a type of biological catalyst that aids in the acceleration of chemical reaction.…

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Biochemistry

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ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

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Problem 1P

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An enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a keat value of 181 s1. At an initial enzyme concentration of 0.0100 µM, the initial reaction velocity was found to be 1.07 x 10-0 µM/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) ? [S] !! µM Submit
From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.
From a kinetics experiment, kcat was determined to be 295sec-1. For the kinetic assay, 0.3mL of a 0.25mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 3mL. Calculate Vmax (µM∙min-1) for the enzyme and catalytic efficiency ( in M-1sec-1) for the enzyme. The Km for the enzyme was determined to be 2.55 x 10-2M.
From a kinetics experiment, Kcat was determined to be 55sec^-1. For the kinetic assay, 0.05mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 30,000g/mole. Assume a reaction volume of 3mL. Calculate Vmax (um*min^-1) for the enzyme and catalytic efficiency (in M^-1sec^-1) for the enzyme. The Km for the enzyme was determined to be 8.3*10^-2M.
A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).
An enzyme-catalyzed reaction is allowed to proceed for 3.4 minutes under steady-state conditions (with large excess of substrate). If the enzyme concentration is 7.9 nM, and the concentration of product formed is 6.3 µM, what is the kcat of this enzyme? Please give your answer to two significant figures in s1.
In your acid phosphatase enzyme kinetics lab, you constructed a Lineweaver-Burk plot. Lefs assume that you graphicaly obtain 1/Vmax - 9.33 (umoliey and -1Km--0.012 M. Which of the following is correct? A) Vmax = 9.33 (no units) B) Km = 0.012 (no units) C) Vmax = (1/Vru" = 0.107 umolis D) Km =-14-1K = 83.3 pM E) Both C) and D) are correct
During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.
An enzyme catalyzes a reaction at a velocity of 20 μmol/min when the concentration of substrate (S)is 0.01 M. The Km for this substrate is 1 × 10-5 M. Assuming that Michaelis-Menten kinetics arefollowed, what will the reaction velocity be when the concentration of S is 1 ×10-6 M?
If Vmax for a reaction is 10 μM ⋅ s-1 and the KM is 0.5 μM, what is the reaction velocity when the substrate concentration is 2 μM?
An enzyme catalyzes a reaction at a velocity of 20 micromole/min when the concentration of substrate (S) is 0.01 M. The Km for this 1 X 10^-5 M. Assuming that Michaelis-Menten Kinetics are followed, what will the reaction velocity be when the concentration of S is 1.0 X 10^-6 M?
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.

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