Both plots are used in enzyme kinetics
A Michaelis-Menton Plot looks like this:
And it is the representation of the equation:
were:
v = reaction rate = the rate at which your product (the product of the enzymatic reaction) is forming
[S] = the concentration of the substrate
Vmax = the maximum reaction rate = this rate is equal to the saturation of the system were all the available enzyme is pair whit a substrate. And therefore can't go any higher.
Km = Michaelis - Mente constant = Vmax/2
So on your data you could find a point were the v/product formation does not go any higher, that would be your Vmax and you could know your Km
A Lineweaver-Burke Plot is a different take on the Michaelis-Menton Plot in which we change the equation so your v plots in a straight line;
were:
v = reaction rate = the rate at which your product (the product of the enzymatic reaction) is forming
[S] = the concentration of the substrate
Vmax = the maximum reaction rate = this rate is equal to the saturation of the system were all the available enzyme is pair whit a substrate. And therefore can't go any higher.
Km = Michaelis - Mente constant = Vmax/2
And the plot look like:
Whit your data you should be able to find Vmax and there fore find Km
Where do the numbers come from for a Michaelis-Menton and Lineweaver-Burke Plot? Can you please explain...
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...
What would a Michaelis Menton Plot and a Lineweaver-Burke plot look like using this data? Use this data for your Test 1 results: Table 1.0 Enzyme concentration Trial 1 (sec) Trial 2 (sec) Enzyme Concentration (Units/mL) 100 units/mL 75 units/mL 50 units/mL 25 units/mL. | 10.30 sec 9.14 sec 8.78 sec 7.50 sec 9.85 sec 8.70 sec 7.72 sec 7.36 sec I'll need to use the average amount of each trial to calculate the rate (1/sec).
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
5.How would you determine the values of KM and Vmax from a: a) Michaelis-Menten plot b) Lineweaver-Burke plot 6. How is general acid/base catalysis different from regular acid/base catalysis? 7. How would you recognize the process of covalent catalysis in an enzyme reaction mechanism?
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
i need help with all question 5 please! thank you Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
How can the Michaelis-Menten constant, be derived from this Lineweaver-Burk plot? Vmax O km = (-1)/(x-intercept) O km = (-1) * (x-intercept) O km = 1/(x-intercept) 0 Km = s;lope
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
Please do everything like you were answering a test. Don’t attempt if youre not going to do all parts. Do it ASAP and I will give you a good rating. If not I will report you. Thank you so much for being the best. Show work if necessary and be concise. There’s no way for me to separate so do all parts. do all parts please. I cant seperate it because it will be refunded. 2. i) (10 points) The...