Sol.
Michaelis-Menten(M-M) equation :
V₀ = Vmax [S] / ( KM + [S] )
So , in M-M plot , we plot V₀ vs [S]
Lineweaver - Burk(L-B) equation :
1/V₀ = ( KM / Vmax )*1/[S] + 1/Vmax
So , in L-B plot , we plot 1/V₀ vs 1/[S]
In L-B plot , equation of line ,
y = 13.77x +3.025
So , 1/Vmax = 3.025
and , Vmax = 1/3.025 = 0.33057 mM / s
Also , from equation of line ,
KM / Vmax = 13.77
KM = 13.77*0.33057 = 4.55194 mM
Also , Kcat = Vmax / [E]
As total enzyme concentration = [E] = 5 M = 0.005 mM
So , Kcat = 0.33057 / 0.005 = 66.114 s-1
Kcat / KM = 66.114 / 4.55194 = 14.52435 mM-1 s-1
Michaelis-Menten plot and Lineweaver-Burk plot calculations- use provided data to generate both M-M and L-B plots....
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots. Use scatter plots with markers on Excel: On the M-M Plot: estimate Vmax, KM On the L-B Plot: determine Vmax, KM, keat, kcat/Km. The total enzyme concentration is 5 uM. Graphs can be 1/2 page. Must be computer generated with all axes labeled. Substrate (mM) V. (mM/s) | 1/[S] (mM1) 1/V. (s/mM) 10 | 0 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228...
(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...
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each plot, demonstrating how Km and Vmax can be determined. On the same graphs, draw another plot where the same enzyme-catalyzed reaction is subjected to inhibition by a competitive inhibitor.
2. If an inhibitor competitively inhibits an enzyme, use Michaelis-Menten and Lineweaver-Burk plots to illustrate how the enzyme kinetics differ in the presence and absence of the inhibitor. (20 pts)
In kinetics experiments, the hydrolysis of the substrate sialic acid by neuraminidase appears to obey Michaelis–Menten kinetics. Neuraminidase activity is critical for viral infectivity; thus, this enzyme is the target of much work by pharmaceutical companies to develop a drug to treat influenza virus infection. The drug “Tamiflu” is a competitive inhibitor of neuraminidase. Initial rate data collected at pH=6.15, 37 ∘C with 0.021 μM neuraminidase and 25.0 μM sialic acid gives a Lineweaver–Burk plot with a slope of 51.2...
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