For an enzyme that follows the Michaelis-Menten kinetic, what substrate concentrations (relative to Km) are needed...
For an enzyme that follows the Michaelis-Menten kinetic, what substrate concentrations (relative to Km) are needed for the speed of the reaction to be
- 0.12 there vmax
- 0.25 there vmax
- 0.5 there vmax
- 0.9 there vmax.
Homework Answers
![solution The michaelis-menten equation is given by ZZZZZZLL2222 Umax [s] 7= kent [s] re speed of reaction Vmax= maximum rate.](http://img.homeworklib.com/questions/7ca6cc20-71db-11ea-bb0d-b3321e412197.png?x-oss-process=image/resize,w_560)
![km X0 12 = 0.88* [s] = 0.12 kmat - 0.136 km 10.88 [s] = D.186 km And r - 0.25 Vmax Hence, 0.25 = 1ST Kent [s] 0.25km +0.25 [s](http://img.homeworklib.com/questions/7d88f500-71db-11ea-a1dc-273ffc67ffeb.png?x-oss-process=image/resize,w_560)
![HIFFHHHHHFFFFFFFFFFEE (C) = 0.5 U max [s] Hence, 0.5= kon + [s] 0.5x kas & 0.5 [s] = [s] 0.5 ks = 0.5 [s [s] = km Ane (d) r=](http://img.homeworklib.com/questions/7e634660-71db-11ea-97cb-7ff1426f3676.png?x-oss-process=image/resize,w_560)
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For an enzyme that follows the
Michaelis-Menten kinetic, what substrate concentrations (relative
to Km) are needed...
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...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed react...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
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
An enzyme follows Michaelis-Menten kinetics. Indicate (with an "x") which of the kinetic parameters would be...
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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 _________
What is the velocity of a Michaelis-Menten enzyme reaction (in terms of vmax) when the concentration...
What is the velocity of a Michaelis-Menten enzyme reaction (in terms of vmax) when the concentration of substrate is 4 times the value of KM? Show your work.
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)
will rate thanks Q1. WHAT ARE ENZYMES? HOW DOES ENZYME-SUBSTRATE BINDING TAKES PLACE? Q2. IN MICHAELIS...
will rate thanks
Q1. WHAT ARE ENZYMES? HOW DOES ENZYME-SUBSTRATE BINDING TAKES PLACE? Q2. IN MICHAELIS -MENTEN GRAPH, WHY DOES THE CURVE REACHES PLATEAU? Vmax Reaction velocity (v) Vm/2 Km Substrate concentration (S) Q3. IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax? Q4. SMALLER VALUE OF THE MICHAELIS CONSTANT (Km) REFLECTS HIGHER EFFICIENCY OF THE ENZYME. (TRUE/FALSE).
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
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
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...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
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)
will rate thanks
Q1. WHAT ARE ENZYMES? HOW DOES ENZYME-SUBSTRATE BINDING TAKES PLACE? Q2. IN MICHAELIS -MENTEN GRAPH, WHY DOES THE CURVE REACHES PLATEAU? Vmax Reaction velocity (v) Vm/2 Km Substrate concentration (S) Q3. IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax? Q4. SMALLER VALUE OF THE MICHAELIS CONSTANT (Km) REFLECTS HIGHER EFFICIENCY OF THE ENZYME. (TRUE/FALSE).
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
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
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