The Lineweaver-Burke Plot for the enzyme in question 1 is shown below. In this plot, the y intercept (0.019153) is 1/vmax and the x intercept (-0.0449) is -1/km.
Km=
Vmax=
Y Intercept 1/Vmax = 0.019153
Vmax = 1 / 0.019153 = 52.21
Y Intercept -1/Km = -0.0449
Km = 1/ 0.0449 = 22.27
The Lineweaver-Burke Plot for the enzyme in question 1 is shown below. In this plot, the...
3.) Enzyme concentration is 3nmol/mL, a Lineweaver-Burke plot of the data gives a line of y = 0.52870x + 0.00426 where the y intercept has units of umol' mL s. [S] uM vo (umol ml-15-1) 169 320 160 132 80.0 92.0 40.0 57.2 20.0 32.6 10.0 17.5 Calculate kcat for the reaction. Calculate Km for the enzyme.
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk plot. You determine the X-intercept is at -0.02 mM-1 and the Y-intercept is at 5.0 (mM/sec)-1. Calculate the Vmax and Km for this enzyme. A. Vmax = 0.20 mM/sec; Km = 50.0 mM B. Vmax = 0.20 mM/sec; Km = ‒50.0 mM C. Vmax = 5.0 mM/sec; Km = 0.02 mM D. Vmax = 5.0 mM/sec; Km = ‒0.02 mM
Where do the numbers come from for a Michaelis-Menton and Lineweaver-Burke Plot? Can you please explain in detail please and thank you? Did an Enzyme lab w/dilutions and recorded absorbances. I am now asked to construct Michaelis-Menton ans Lineweaver-Burke plots BUT I dont know if the plot is based on my results from the dilutions and absorbances. For your lab reports, you will determine how much sugar was made during your enzyme reactions in Week 2 based on the linear...
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
3. Below is a Lineweaver-Burke plot of an enzyme reaction in the presence and absence of an inhibitor. 2.4 2.3 2.2 2.1 2 1.9 1.8 1.7 1.6 1.5 1.4 1.3 1.2 1.1 1 0.9 0.8 < 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 -0.1 -0.2 -0.3 -0.4 -0.5 -0.6 -0.7 -0.8 . . . . . -1 -0.9 -0.8 -0.7 -0.6 -0.5 -0.4 -0.3 -0.2 -0.1 O 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 1.1 1/[S]...
please graph all 3 lines and explain the vmax&km How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
Biochemistry inhibitors! Pls answer 1 through 11 For each of the following items, indicate whether the item pertains to: • Competitive inhibitor . Uncompetitive inhibitor • Noncompetitive inhibitor • Noncompetitive activator • None of the above Choose only one of the above for each item. 1. Binds to the enzyme-substrate complex only 2. Prevents substrate from binding enzyme 3. Forms inactive El or inactive ESI complex 4. When present, Vmax increases 5. When present, Vmax increases and Km decreases 6....
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menton plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. see for instance: http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 1 µM and a different variant has a Km of 10 µM....
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...