Homework Answers
1. Yes, the relationship is linear. The initial reaction rate increases as the substrate concentration increases. With more substrates, there will be a more of the reaction ocuring, as there is more to be used up. As the initial reaction rate increases it goes faster.
3. the maximum initial reaction rate cannot be reached at low substrate concentrations because there is not enough substrate .
5. Enzymes change shape at higher temperatures and then reaction cannot happen .
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fect Journal Describe the relationship between substrate concentration and the initial reaction rate of an...
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 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...
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial...
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial rate, Ms SJ, M 0.020 0.585 0.004 0.495 0.002 0.392 0.001 0.312 0.250 0.00066 Determine Vmax and Km for this reaction
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,...
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 V for...
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 E S E+P. The model can be more readily understood when comparing three conditions: (S) <<K.. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V, where steady state conditions are assumed. Etotal) refers to the total enzyme concentration and Etree refers to the concentration...
You measure the initial rate of an enzyme reaction as a function of substrate concentration in...
You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: Create a Michaelis-Menten plot (inhibited and uninhibited should be on the same plot! You MUST use Excel and follow the provided instructions "Non-Linear Regression Fitting of Kinetics Data". Calculate the V_max in the presence and absence of the inhibitor. Calculate the K_m in the presence and absence of the inhibitor. What type...
The Arrhenius equation shows the relationship between the rate constant k and the temperature T in...
The Arrhenius equation shows the relationship between the rate constant k and the temperature T in kelvins and is typically written as k=Ae−Ea/RT where R is the gas constant (8.314 J/mol⋅K), A is a constant called the frequency factor, and Ea is the activation energy for the reaction. However, a more practical form of this equation is lnk2k1=EaR(1T1−1T2) which is mathmatically equivalent to lnk1k2=EaR(1T2−1T1) where k1 and k2 are the rate constants for a single reaction at two different absolute...
The Arrhenius equation shows the relationship between the rate constant k and the temperature T in...
The Arrhenius equation shows the relationship between the rate constant k and the temperature T in kelvins and is typically written as k=Ae−Ea/RT where R is the gas constant (8.314 J/mol⋅K), A is a constant called the frequency factor, and Ea is the activation energy for the reaction. However, a more practical form of this equation is lnk2k1=EaR(1T1−1T2) which is mathmatically equivalent to lnk1k2=EaR(1T2−1T1) where k1 and k2 are the rate constants for a single reaction at two different absolute...
how do I draw graph for this? collisions between ernzyme and substrate is tion rate. Sketch...
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
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 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...
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial rate, Ms SJ, M 0.020 0.585 0.004 0.495 0.002 0.392 0.001 0.312 0.250 0.00066 Determine Vmax and Km for this reaction
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,...
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 V for an enzyme-catalyzed, single-substrate reaction E+S E S E+P. The model can be more readily understood when comparing three conditions: (S) <<K.. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V, where steady state conditions are assumed. Etotal) refers to the total enzyme concentration and Etree refers to the concentration...
You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: Create a Michaelis-Menten plot (inhibited and uninhibited should be on the same plot! You MUST use Excel and follow the provided instructions "Non-Linear Regression Fitting of Kinetics Data". Calculate the V_max in the presence and absence of the inhibitor. Calculate the K_m in the presence and absence of the inhibitor. What type...
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
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