- Vmax is a kinetic property associated with an enzyme. Describe what occurs when an enzyme reaches its Vmax.
- Km is also another intrinsic property of an enzyme. Practically, what does the Km tell about how an enzyme interacts with its substrate?
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- Vmax is a kinetic property associated with an enzyme. Describe what occurs when an enzyme...
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot Vo versus (substrate), or 1/Vo versus 1/[substrate], how the curves would look like, and how to get Vmax and Km values?
1. Define Vmax and Km (Michaelis constant). What is the mathematical relationship between these two values? 2.What does Km tell you about the affinity of an enzyme for its substrate? 3.Why do we use the slope between the first two data points of Absorbance vs Time to determine V0 when studying enzyme kinetics? Why not use the slope of the entire line?
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.
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
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 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...
You are studying a new muscle enzyme, M, and need to characterize its kinetic properties. a) Experimentally, how will you determine the M’s VMAX and KM for its substrate , A? EXPLAIN in detail, including any limitations your mathematical methods may have. b) Now consider that it is known that another molecule, D, also binds to M, and interferes with the reaction that converts A to product Q, but you don't know where or how. What kind of kinetic evidence...
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).
Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to the formation of acyl enzyme intermediate. Specify the role of each of the amino acids in the catalytic triad. B) Provide a Michaelis-Menten rate-law equation. Subsequently, on the same graph draw Lineweaver-Burk plots for i) enzyme which is not inhibited: ii) enzyme inhibited by a non-competitive inhibitor, C) The Km and kcat for hexokinase with as a glucose substarte are 5-10 M and 8-10²...
b. For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: a. [S] Km b. S] 0.1 Km c. [S] 50Km c. What will be the initial velocity (yo) for an enzyme that has Km 2.5 [S]? Your answer will be a fraction of Vmax a.