Examine the formula for the kinetics of a ping-pong bisubstrate reaction, 1/v = (KmA / Vmax)(1/[A])...
Examine the formula for the kinetics of a ping-pong bisubstrate reaction, 1/v = (KmA / Vmax)(1/[A]) + (1 + KmB/[B])(1/Vmax) Show that for high concentrations of [B], particularly [B] >> KmB, this equation reduces to the ordinary Lineweaver-Burk formula for the other substrate, A.
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Examine the formula for the kinetics of a ping-pong bisubstrate
reaction, 1/v = (KmA / Vmax)(1/[A])...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
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...
This wuestion has parts to it. I will rate. 1. 2. 3. 4. If a reaction...
This wuestion has parts to it. I will rate.
1.
2.
3.
4.
If a reaction is zero-order in a reactant, when the concentration of the reactant is decreased by a factor of 2, the reaction rate will: 。Adecrease by a factor of 1/2· 0 B. remain constant. C. double. O D. quadruple. OE. decrease by a factor of 1/4 You are working with a nonallosteric enzyme that displays Michaelis-Menten kinetics. At what percent of the maximum velocity wll the...
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 _________
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
(1 point) A ping-pong ball is caught in a vertical plexiglass column in which the air...
(1 point) A ping-pong ball is caught in a vertical plexiglass column in which the air flow alternates sinusoidally with upward flow at the rate of 3.3m/s and at t = 30 seconds the flow has a minimum (upward) flow of rate of -5.9m/s. (To make this clear: a flow of -5m/s upward is the same as a flow downward of 5m/s. period of 60 seconds. The air flow starts with a maximum The ping-pong ball is subjected to the...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as...
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...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
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...
This wuestion has parts to it. I will rate.
1.
2.
3.
4.
If a reaction is zero-order in a reactant, when the concentration of the reactant is decreased by a factor of 2, the reaction rate will: 。Adecrease by a factor of 1/2· 0 B. remain constant. C. double. O D. quadruple. OE. decrease by a factor of 1/4 You are working with a nonallosteric enzyme that displays Michaelis-Menten kinetics. At what percent of the maximum velocity wll the...
(1 point) A ping-pong ball is caught in a vertical plexiglass column in which the air flow alternates sinusoidally with upward flow at the rate of 3.3m/s and at t = 30 seconds the flow has a minimum (upward) flow of rate of -5.9m/s. (To make this clear: a flow of -5m/s upward is the same as a flow downward of 5m/s. period of 60 seconds. The air flow starts with a maximum The ping-pong ball is subjected to the...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
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...
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