. Derive an equation expressingv/Vmax\1-v/Vmax.as a function of log[S]for an enzyme that obeys the Michaelis-Menten equation.For an allosteric enzyme, show how you could use this equation toobtain K and K (the KM values for T and R states) from a Hill plotof kinetic data

An enzyme is a biocatalyst, which reduced the activation energy and increase velocity of a…

Answered: . Derive an equation expressing v/Vmax…

Chemistry

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ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
A An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181 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
In a Lineweaver-Burk plot of enzyme kinetic data, the x-intercept is –2.5 mM-1, what is the Km of the enzyme
The enzyme-catalysed conversion of a substrate at 25 oC has a Michaelis constant of 0.015 mol dm-3 . and a max-imum velocity of 4.25 x 10-4 mol dm-3 s-1 when the enzymeconcentration is 3.60 x 10-9 mol dm-3. Calculate koat and the catalytic efficiency η. Is the enzyme 'catalytica lly perfect'?
Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? Calculate Vmax of the above enzyme (lactase). Calculate the slope on a Lineweaver-Burk plot (Km/Kmax) for the above enzyme (lactase).
An enzyme kinetics experiment is carried out by adding 1.00mg of a 50.0kDa enzyme into a total volume of 50uL of buffer, and measuring the initial rates while adding increasing amounts of substrate (1 Da = 1 g/mol). The calculated Vmax from this series of experiments was 30.5mM/s. Calculate the turnover number for the enzyme.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 micrograms/micromole; 8 micrograms of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?
When studying the inhibition kinetics of a certain enzyme, the results have been obtained from the following table: Determine graphically:a) the type of inhibition b) the KM value of the enzyme c) the maximum speed of this experiment d) the value of Ki.
Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation. a)At what substrate concentration would an enzyme with a kcatof 30.0 s-1and a Kmof 0.0050 M operate at one-quarter of its maximum rate? b)Determine the fraction of Vmax that would be obtained at the following substrate concentrations [S]:1/2Km,2Km,and10Km. c)An enzyme that catalyzes the reaction X ßàY is isolated from two bacterial species. The enzymes have the same Vmax, but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, while enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X]=1 μM. Which curve corresponds to which enzyme?
An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 Calculate the Km of the enzyme in the reaction without inhibitor ________________________ Km’ of the enzyme in the reaction with inhibitor ________________________ Vmax of the uninhibited reaction ________________________ Vmax’ of the inhibited reaction ________________________

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. Derive an equation expressing v/Vmax \1-v/Vmax. as a function of log[S] for an enzyme that obeys the Michaelis-Menten equation. For an allosteric enzyme, show how you could use this equation to obtain K and K (the KM values for T and R states) from a Hill plot of kinetic data