A single-substrate enzyme that obeys Michaelis-Menten kinetics displays the following parameters: Kd = 3.1 x 10^-5...
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.
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A single-substrate enzyme that obeys Michaelis-Menten kinetics
displays the following parameters: Kd = 3.1 x 10^-5...
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and...
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity v (as a percentage...
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 _________
In the absence of allosteric effectors, the enzyme phosphofructokinase displays Michaelis–Menten kinetics (see Fig. 7.15). The...
In the absence of allosteric effectors, the enzyme phosphofructokinase displays Michaelis–Menten kinetics (see Fig. 7.15). The v0/Vmax ratio is 0.9 when the concentration of the substrate, fructose-6-phosphate, is 0.10 mM. Calculate the KM for phosphofructokinase under these conditions (in units of mM).
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the ...
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM
b. For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: a. [...
b. For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: a. [S] Km b. S] 0.1 Km c. [S] 50Km c. What will be the initial velocity (yo) for an enzyme that has Km 2.5 [S]? Your answer will be a fraction of Vmax a.
An enzyme that follows Michaelis-Menten kinetics has a initial velocity of 300 nM/s at a substrate...
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
An enzyme follows Michaelis-Menten kinetics. Indicate (with an "x") which of the kinetic parameters would be...
An enzyme follows Michaelis-Menten kinetics. Indicate (with an "x") which of the kinetic parameters would be altered in the presence of the corresponding type of inhibitors. Inhibitor type Vmax Km Neither Both Competitive Uncompetitive Noncompetitive
In kinetics experiments, the hydrolysis of the substrate sialic acid by neuraminidase appears to obey Michaelis–Menten...
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...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the...
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 ...
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...
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM
b. For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: a. [S] Km b. S] 0.1 Km c. [S] 50Km c. What will be the initial velocity (yo) for an enzyme that has Km 2.5 [S]? Your answer will be a fraction of Vmax a.
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
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...
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