
![1-07X10-544 +1.07 X10-6c83; = 2.0165); 2.01[s] =7.67X1026[s]; 1007 X10-5 41 = 1007 X10-5 4M- 2.00 [5]; [s];= 1-07X10-54M - a](http://img.homeworklib.com/questions/1a5346d0-ebb3-11eb-8113-0fcaeda74f39.png?x-oss-process=image/resize,w_560)
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and...
An enzyme that follows Michaelis-Menten kinetics has a KM value of 20.0 μM and a kcat value of 211 s−1. At an initial enzyme concentration of 0.0100 μM, the initial reaction velocity was found to be 1.07×10−6 μM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures.
1)
2) If the total enzyme concentration was 9 nmol/Lnmol/L, how
many molecules of substrate can a molecule of enzyme process in
each minute?
Express your answer to three significant figures.
3) The kcat for neuraminidase at pH=6.15pH=6.15, 37 ∘C∘C is 26.8
s−1s−1. Calculate KMKM for the hydrolysis of sialic acid.
Express your answer with the appropriate units.
An enzyme that follows Michaelis-Menten kinetics has a Ky value of 6.00 uM and a keat value of 176 s-1. At an...
An enzyme that follows Michaelis-Menten kinetics has a initial velocity of 300 nM/s at a substrate concentration of 30 uM. The maximum velocity of 400 nM/sec. What is the Km for this enzyme in uM? (Give your answer as a number only. Type your response
A single-substrate enzyme that obeys Michaelis-Menten kinetics displays the following parameters: Kd = 3.1 x 10^-5 M; k1 = 107 M-1 s-1, and kcat = 10^4 s-1. Given this information, what is the value of the Michaelis constant Km? Express your answer in terms of mM to four significant figures.
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
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...
(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...
9. Applying the Michaelis-Menten Equation I An enzyme catalyzes the reaction A = B. The enzyme is present at a con- centration of 2 nm, and the Vmax is 1.2 ums". The Km for substrate A is 10 um. Calculate the initial velocity of the reaction, Vo, when the substrate concentration is (a) 2 um, (b) 10 um, (C) 30 um.
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 _________
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of Happyase for its substrate ICE is Km^s = 1mM. Happyase also acts on substrate CREAM and its Km^T =10mM. Is ICE or CREAM the preferred substrate for Happyase? Explain b. The rate constant k2 with substrate ICE is 2x10^4sec^ -1; with substrate CREAM, k2=4x10^5sec ^-1. Does Happyase use substrate ICE or substrate CREAM with greater catalytic efficiency? Show calculations and explain your answer