(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 initial velocity if the substrate concentration is 0.74 mol/L.
a) From the graph of Velocity vs Substrate concentration, we have the following conclusions:
1) If the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will increase until it reaches a maximum. After this point, increases in substrate concentration will not increase the velocity.
2) KM (Michaelis constant) is the substrate concentration at half the maximum velocity.
From the graph given below VMax = 0.66
Vmax/2 = 0.33
KM = 0.51
b) The graph of 1/v vs 1/S has the following points: (0.67, 1.51), (0.83, 1.54), (1.23, 2.22), (1.53, 2.56), (2.04, 3.13), (3.7,4.76)
The graph is given below
c) From the first graph, when S= 0.74, we get initial velocity is 0.42 mM/min
(15 points) The following data is for a reaction catalyzed by tyrosine monoxygenase: Substrate Concentration (mol/L) ...
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...
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial rate, Ms SJ, M 0.020 0.585 0.004 0.495 0.002 0.392 0.001 0.312 0.250 0.00066 Determine Vmax and Km for this reaction
The following data set was collected from an experiment conducted in the lab where a new enzyme is being characterized. Use the Lineweaver-Burk method in order to determine the values of KM and Vmax. Complete your work on a separate piece of paper and upload the excel file or picture of your work. Your work must include the following: Table of reciprocals Reciprocal plot (straight-line graph) Calculations and results for KM and Vmax In order to get full credit for...
8. The initial rate for an enzyme-catalyzed reaction has been deter mined at a number of substrate concentrations. Data are as follows: (Sl (pmol/L) (pmol/L) min) 65 102 120 135 200 (a) Estimate Vmax and Ky from a direct graph of y versus (SI (these data are plotted in Figure 11.246). Do you find difficulties in get- ting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better? 8. The initial rate for...
Consider the enzyme-catalyzed reaction with Vmax=164 (μmol/L)min−1 and KM=32μmol/L. Part A If the total enzyme concentration was 6 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures. kcat kcat = 2.73×104 min−1 Part B Calculate kcat/KM for the enzyme reaction.
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...
1.5 1.9 2.0 2.1 22 2.3 24 25 26 2.7 28 3) (a) An enzyme is used to convert a substrate at a temperature of 25°C. The Michaelis constant of this reaction is 0.042 mol dm3. The velocity of the reaction is 2.45 x 104 mol dm s when the substrate concentration is 0.890 mol dm3. Find the maximum velocity of this reaction? hint: vk2Er +161 and vmax (b) Plot v - vs -[S] for a standard enzymatic reaction that...