3. In an enzyme-catalzed reaction, Vmax=0.2mol/sec and Km=5mM. a) What is the rate of the reaction...
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...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
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.)
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...
For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity v (as a percentage of Vmax) ,observed at each of the following substrate concentrations. (Ex, v = xVmax, where x = an integer, fraction, or decimal number (two decimal places)) a) [S] = 0.1 Km _________ b) [S] = 2 Km _________ c) [S] = 10 Km _________
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
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....
1. Define Vmax and Km (Michaelis constant). What is the mathematical relationship between these two values? 2.What does Km tell you about the affinity of an enzyme for its substrate? 3.Why do we use the slope between the first two data points of Absorbance vs Time to determine V0 when studying enzyme kinetics? Why not use the slope of the entire line?
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
1.5 1.9 2.0 2.1 22 2.3 24 25 26 2.7 28 3) (a) An enzyme is used to convert a substrate at a temperature of 25°C. The Michaelis constant of this reaction is 0.042 mol dm3. The velocity of the reaction is 2.45 x 104 mol dm s when the substrate concentration is 0.890 mol dm3. Find the maximum velocity of this reaction? hint: vk2Er +161 and vmax (b) Plot v - vs -[S] for a standard enzymatic reaction that...