Graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction. However, these quantities can sometimes be estimated by inspecting values of Vo at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the data in the table were obtained. [S] (M) Vo (uM min-1) 2.5 x 10-6 28 4.0 × 10-6 40 1 x 10-5 70 2 x 10-5 95 4 x 10-5 112 1 x 10-4 128 2 x 10-3 139 1 × 10-2 140 Please enter your answers using values from the table. Use a whole number for Vmax : 70 Vmax µM min- Incorrect

Graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction. However, these quantities can sometimes be estimated by inspecting values of Vo at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the data in the table were obtained. [S] (M) Vo (uM min-1) 2.5 x 10-6 28 4.0 × 10-6 40 1 x 10-5 70 2 x 10-5 95 4 x 10-5 112 1 x 10-4 128 2 x 10-3 139 1 × 10-2 140 Please enter your answers using values from the table. Use a whole number for Vmax : 70 Vmax µM min- Incorrect

Fundamentals Of Analytical Chemistry

9th Edition

ISBN:9781285640686

Author:Skoog

Publisher:Skoog

Chapter34: Miscellaneous Separation Methods

Section: Chapter Questions

Problem 34.19QAP

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An enzyme-catalyzed reaction has a Km of 1 mM and a Vmax of 4 nmole/L sec-1. The reaction velocity (nmole/L sec-1) when the substrate concentration is 0.25 mM is: A. 1.25 B. 10.0 C. 5.0 D. 0.50 E. 1.0 F. 100 G. 150 H. 55 I. 75
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
Although there are accurate graphical methods available for determining Vmax and Km of an enzyme-catalyzed reaction, sometimes these parameters can be quickly estimated by examining the values of Vo as [S] increases. Estimate the values of Vmax and Km of the reaction catalyzed by an enzyme in which the following data were obtained:
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).
If 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, calculate the new Vmax. Calculate the new Km of the above lactase reaction, with inhibitor X. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. Inhibitor X exerts which of the following effects on the above enzyme (lactase)?
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 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
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
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 ________________________
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?
Determine the value of the turnover number of the enzyme catalase, given that RmaxRmax (Vmax)(Vmax) for catalase is 41 mmol⋅L−1⋅s−141 mmol⋅L−1⋅s−1 and [E]t[E]t equals 4.8 nmol⋅L−14.8 nmol⋅L−1 . Catalase has a single active site.
The first-order degradation rate constant k was determined to be 0.0125/day for contaminant A and 0.0030/day for contaminant B in a soil. Calculate the half-life T1/2 and the 95% dissipation time for these contaminants in the soil. Compare the persistence between the two contaminants.