Understanding enzyme kinetics - Henri-Michaelis-Menten model

An enzyme with a Km of 0.36 mM was assayed using substrate concentrations of 3 x 10E-7 M, 9.5 x 10E-5 M, 1.5 x 10E-4, 1.16x10E-3, 3 x 10E-3 M, 0.01 M, 0.08 M. At a substrate concentration of 0.08 M, the initial velocity was 192 nM/min. Calculate the initial velocity at each of the other substrate concentrations. Graph the calculated velocities using the Henri-Michaelis-Menten model.

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Problem:

An enzyme with a Km of 0.36 mM was assayed using substrate concentrations of 3 x 10E-7 M, 9.5 x 10E-5 M, 1.5 x 10E-4, 1.16x10E-3, 3 x 10E-3 M, 0.01 M, 0.08 M. At a substrate concentration of 0.08 M, the initial velocity was 192 nM/min. Calculate the initial velocity at each of the other substrate concentrations. Graph the calculated velocities using the Henri-Michaelis-Menten model.

Solution:

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Solution Summary

The solution contains a complete description of how to approach this type of enzyme kinetics question. The Henri-Michaelis-Menten equation is explained, and each of the variables in the equation are defined. The solution also contains several important tips for avoiding common mistakes, including unit analysis.

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[S](mM) ----------------- 0.33 10.00
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I carried out a practical last week and need to write it up but canot remember how to do the calculations from the Michaelis-Menten graph plotted which I guess helps me to plot a Lineweaver-Burk.
I have attached the practical requirements.
I have to produce a table (attached) but cannot fill in certain columns until I can work

You characterize a new enzyme's kinetics. Using a saturating (very high so all E is ES) substrate concentration, you measure the initial rate of the reaction at various enzyme concentrations. Does this data fit the Michaelis Menton model/equation? If not, what may be happening?
E (nM), rate (mM,s)
5, 50
10, 225
15

See the attached .doc
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A) What is the initial velocity v0 called when the substrate concentration [S] >>>KM ([S] )?
Label on graph.
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Phosphofructokinase is an enzyme, widespread in nature, catalyzing the reaction:
fructose-6-phosphate + ATP ----> fructose-1,6-diphospohate + ADP
Under conditions where the concentration of ATP was held constant, the dependency of the initial velocity of the concentration of fructose-6-phosphate as measured at two differen

(See attached file for diagrams)
1. For a Michaelis-Menten reaction, k1 = 5 x 107 M-1 s-1, k-1 = 2 x 104 s-1, and k2 = 4 x 102 s-1. Calculate Ks and Km for this reaction. Does substrate binding achieve equilibrium or the steady state?
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For a MM reaction
k1=5x10^7
k-1=2X10^4
k2=4x10^2
i calculated Km and Ks to be equal at about 4 x10^-4M
Does substrate binding achieve equilibrium or the steady state?
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A) Using the data given in table below plot a Lineweaver-Burk plot
b) Determine the Km and Vmax for the three sets of data
c) Which inhibitor would the most effective at high substrate concentrations?
d) Explain you choice
Table 1 :
Kinetics data for an enzyme catalysed reaction with and without the presence of