Calculate the velocity of an uninhibited enzyme catalyzed reaction using the following with the Michaelis-Menton equations:
Km= 3x 10^-8
[S]= 1/2 Km
Vmax= 5.0 nmole/L*sec
Et= 2.0 x10^-10 M
Calculate the velocity of an uninhibited enzyme catalyzed reaction using the following with the Michaelis-Menton equations:...
Use the Michaelis-Menton equation, what is the velocity of an uninhibited enzyme (catalyzed reaction)? What is the enzyme’s turnover number given the following data: Km=4x10 ^-8M ; [S]=½ Km ; Vmax= 6.0 nmole/L•sec ; Et=1.0x10 ^ -10M.)
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
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....
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...
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very low concentrations of substrate (Km is greater than S) the Michaelis-Menton equation can be simplified to? At very high concentrations of substrate, the Michaelis-Menton equation can be simplified to? How do you determine the initial rate of reaction
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
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...
7. a) In an enzyme catalyzed reaction which follows the Michaelis-Menten kinetics. The substrate concentration (Km, Michaelis constant) needed to reach 50% of the maximum reaction velocity (Vmax) is 20 μΜ. What substrate concentration is required to obtain at least 75% of the maximum reaction velocity? Show the work to get full points. (5 points) b) You want to load 10 μg of protein in 15 μL into one of the 10% polyacrylamide gel well. The protein needs to be...
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...