the rate of a certain enzymatic reaction is 2.18 micromol dm^-3 s^-1 when the overall concentration...
the rate of a certain enzymatic reaction is 2.18 micromol dm^-3 s^-1 when the overall concentration of enzyme is 3.96mmol dm^-3 and the concentration of substance is 0.0400 mol dm^-3. When the substrate concentration is increased to 0.100 mol dm ^-3 and the enzyme concentration is unchanged, the rate increase to 3.97 micromol dm ^-3 s^-1. Find the Michaelis constant and the maximum velocity for this enzymatic reaction.
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the rate of a certain enzymatic reaction is 2.18
micromol dm^-3 s^-1 when the overall concentration...
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 reac...
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...
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...
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...
The rate law for a certain enzymatic reaction is zero order with respect to the substrate....
The rate law for a certain enzymatic reaction is zero order with respect to the substrate. The rate constant for this reaction is 4.6 times 10^2 M middot s^-1. If the initial concentration of the substrate is 0.338 mol L^-1, what is the initial rate of the reaction? rate = _______ times 10 _______ M middot s^-1
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
The relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation a) At what substrate concentration would...
The relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation a) At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of 0.0050 M operate at one-quarter of its maximum rate? b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations: [S]=Km/2, [S]=2Km, [S]=10Km
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
The Michaelis-Menten equation models the hyperbolic relationship between [S) and the initial reaction rate V, for a...
The Michaelis-Menten equation models the hyperbolic relationship between [S) and the initial reaction rate V, for an enzyme-catalyzed, single-substrate reaction E+S ES E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> K. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V where steady state conditions are assumed. (E l refers to the total enzyme concentration and [Erre refers...
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate (V0) for...
The Michaelis-Menten equation models the hyperbolic relationship
between [S] and the initial reaction rate (V0) for an enzyme
catalyzed, single substrate reaction: E S ES E P. The model can be
more readily understood when comparing three conditions: [S]Km.
Match each statement with the condition that it describes. Note:
\"Rate\" refers to initial velocity (V0) where steady state
conditions are assumed; [Etotal] refers to the total enzyme
concentration, and [Efree] refers to the concentration of free
enzyme.
categories: [S]<<Km, [S]=Km,...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point...
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)
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
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...
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...
The rate law for a certain enzymatic reaction is zero order with respect to the substrate. The rate constant for this reaction is 4.6 times 10^2 M middot s^-1. If the initial concentration of the substrate is 0.338 mol L^-1, what is the initial rate of the reaction? rate = _______ times 10 _______ M middot s^-1
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
The Michaelis-Menten equation models the hyperbolic relationship between [S) and the initial reaction rate V, for an enzyme-catalyzed, single-substrate reaction E+S ES E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> K. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V where steady state conditions are assumed. (E l refers to the total enzyme concentration and [Erre refers...
The Michaelis-Menten equation models the hyperbolic relationship
between [S] and the initial reaction rate (V0) for an enzyme
catalyzed, single substrate reaction: E S ES E P. The model can be
more readily understood when comparing three conditions: [S]Km.
Match each statement with the condition that it describes. Note:
\"Rate\" refers to initial velocity (V0) where steady state
conditions are assumed; [Etotal] refers to the total enzyme
concentration, and [Efree] refers to the concentration of free
enzyme.
categories: [S]<<Km, [S]=Km,...
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)
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
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