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4. Km, the Michaelis-Menten constant is a composite of three rate constants. What are the three...
The Michaelis and Menten constant, Km is actually a summary of 3 terms:
4.4 For the enzyme reaction:The Michaelis and Menten constant, Km is actually a summary of 3 terms:(a) What are these? (b) What assumption does it make?(c) Define and calculate Km from the above equation given:(d) Which is the rate-limiting step? And why?
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...
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of...
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of Happyase for its substrate ICE is Km^s = 1mM. Happyase also acts on substrate CREAM and its Km^T =10mM. Is ICE or CREAM the preferred substrate for Happyase? Explain b. The rate constant k2 with substrate ICE is 2x10^4sec^ -1; with substrate CREAM, k2=4x10^5sec ^-1. Does Happyase use substrate ICE or substrate CREAM with greater catalytic efficiency? Show calculations and explain your answer
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...
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
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of...
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of Happyase for its substrate ICE is Kms = 1mM. Happyase also acts on substrate CREAM and its Km1 =10mM. Is ICE or CREAM the preferred substrate for Happyase? Explain b. The rate constant k2 with substrate ICE is 2x104sec-1; with substrate CREAM, k2=4x105sec-1. Does Happyase use substrate ICE or substrate CREAM with greater catalytic efficiency? Show calculations and explain your answer.
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.
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
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).
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
4.4 For the enzyme reaction:The Michaelis and Menten constant, Km is actually a summary of 3 terms:(a) What are these? (b) What assumption does it make?(c) Define and calculate Km from the above equation given:(d) Which is the rate-limiting step? And why?
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...
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...
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
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of Happyase for its substrate ICE is Kms = 1mM. Happyase also acts on substrate CREAM and its Km1 =10mM. Is ICE or CREAM the preferred substrate for Happyase? Explain b. The rate constant k2 with substrate ICE is 2x104sec-1; with substrate CREAM, k2=4x105sec-1. Does Happyase use substrate ICE or substrate CREAM with greater catalytic efficiency? Show calculations and explain your answer.
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).
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