Ans :
During the enzyme and substrate are combined and the enzyme is catalzyed the reaction , it will get at particular substrate concentration . When product concentration is linearly increase. The amount of product produced at starting of reaction per unit is known as initial velocity (V0) of the concentration.
Now , the plots for reaction rate
a) a reaction with tight enzyme substrate binding site.
In this plotting reaction are shown below, which are determined information of enzyme kinetics. Here substrate having different concentration when we will add enzyme ( Same concentration).
By the V0 value of all concentration will determine on plotted (X, Y) pair. While in presence of enzyme. it will tightly bind with substrate and form enzyme substance concentration . The V0 value will rapidly increase at low substrate concentration and at high substrate concentration it will flat.
This plotted examine the enzyme is saturated, it mean as that all available enzymes are tighted up with substrate. After that substrate will also wait for another enzyme to trigger reaction. This maximum rate of reaction will determine by Maximum velocity ( Vmax ). Which plotted on Y .
The half way to Vmax of substrate concentration of reaction rate is known as Km. It is used for measure of reaction rate increase with substrate concentration and measure affinity towards enzyme.
Lower Km = higher affinity for substrate
Higher Km = lower affinity for substrate
VMax dependes on enzyme concentration Km which is same for particular enzyme reaction. Km can be changed by inhibitors.
b) a reaction with weak enzyme substrate binding.
Some inhibitors are play role in enzyme substrate binding activity. Such as compititive inhibitor and non compititive inhibitor.
In case of competitive inhibitors trigger reaction by binding to a enzyme at the active site and get the substrate from binding.
When compititive inhibitor bind to the enzyme it will acts by decreasing or weaker the number of enzyme molecules to bind with substrate.
In the graphic reaction Vmax reach normal, when substrate added and the enzymes are inhibits by inhibitors so the effective concentration of enzyme Vmax is reduced and Km is not changed.
The unchanged Km get that inhibitors doesn't affect enzyme binding to substrate at lower concentration of enzyme.
When reaction with weak enzyme substrate binding activity it will get higher Km.
6. (5pts) Draw relative plots for reaction rate as a function of substrate concentration for a)...
(15 points) The following data is for a reaction
catalyzed by tyrosine monoxygenase:
Substrate
Concentration
(mol/L)
Initial Velocity (mM/min)
1.5
0.66
1.2
0.65
0.81
0.45
0.65
0.39
0.49
0.32
0.27
0.21
a) Plot the velocity (y-axis) versus substrate
concentration [S] (x-axis) curve and insert/draw the graph in the
space below. What are the approximate KM and
Vmax values?
b) Construct a 1/v (y-axis) versus 1/[S]
(x-axis) plot in the space below. Calculate the KM and
Vmax values.
c) Calculate the...
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...
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
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 Eadie-Hofstee plot shown below, is an alternative graphical representation of Michaelis-Menten kinetics. t plots the rate (v) versus the ratio of the rate over the substrate concentration (vIS]). This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km Eadie-Hofstee Plot y-intercept Slope x-intercept AS
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...
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...
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 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)
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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).