An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of product/minute/µg...
An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of product/minute/µg of enzyme. After exposure to an inhibitor and analysis on a Lineweaver - Burk plot the following values are obtained: -1/KM = - 0.05 liters/µmole and 1/Vmax = 0.04 (mmoles of product/minute/µg of enzyme)-1. What kind of inhibitor was used in the experiment?
Homework Answers
From the question the Km comes out
to be 1/0.05 = 20 
M and Vmax is 1/0.04
= 25 mmoles of product/min/ug of enzyme. Hence, the Km remains
constant but the Vmax decreases. Hence, this is an example of
reversible noncompetitive inhibition where the inhibitor binds
reversibly to a site other than the active site and causes an
overall change in the three dimensional conformation of the enzyme
that decreases its catalytic activity.
"A malaria biologist"
Add Answer to:
An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of
product/minute/µg...
1-The unmutated form of your protein has a Km of 25 µM and a Vmax of...
1-The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, explain the effect of amino acid substitution on the Km and Vmax for the mutated protein. (Up to 50 words) You are not expected to draw a Lineweaver-Burk plot, however a quick sketch of a Vi vs [S]...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
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...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
The next 3 questions are related. The results of an enzyme analysis are: KM=1.1x10-5 M; VMAX=47.6...
The next 3 questions are related. The results of an enzyme analysis are: KM=1.1x10-5 M; VMAX=47.6 μM/min. What is the Lineweaver Burk plot equation (recall: y=1/Keq and x=1/[S])?
Please show how to calculate Km and Vmax for no inhibitor/low inhibitor given graph. Show how to ...
Please show how to calculate Km and Vmax for no inhibitor/low
inhibitor given graph. Show how to solve for a.,a/a etc.
Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When...
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...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
The following data was obtained for an enzyme in the absence of an inhibitor, and in...
The following data was obtained for an enzyme in the absence of an inhibitor, and in the presence of two different inhibitors. The concentration of each inhibitor was 10 mM. The total concentration of enzyme was the same for each experiment. [S] {mM} without inhibitor v, {umol/(ml*s)} with inhibitor A v, {umol/(ml*s)} With inhibitor B v, {umol/(ml*s)} 0.0 0.0 0.0 0.0 1.0 3.6 3.2 2.6 2.0 6.3 5.3 4.5 4.0 10.0 7.8 7.1 8.0 14.3 10.1 10.2 12.0 16.7 11.3...
ssessable tutorial que 03/2018 The conversion of corn starch to dextrose using the enzyme glucoamylase was...
ssessable tutorial que 03/2018 The conversion of corn starch to dextrose using the enzyme glucoamylase was studied in a batch reactor at 60°C. The initial concentration of corn starch was 25 gl. The dosage of glucoamylase, Eo, was 11.6 mgL-. Figure 1, below, shows a Lineweaver-Burk plot for results obtained for the starch to dextrose enzymatic process. 0.13 0.12 0.11 0.10 Slope of plot 1.1 hr y-intercept of plot-0.033 hr L/g 0.09 0.08 0.07 0.04 0.05 0.06 0.07 0.08 0.09...
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...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
Please show how to calculate Km and Vmax for no inhibitor/low
inhibitor given graph. Show how to solve for a.,a/a etc.
Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
ssessable tutorial que 03/2018 The conversion of corn starch to dextrose using the enzyme glucoamylase was studied in a batch reactor at 60°C. The initial concentration of corn starch was 25 gl. The dosage of glucoamylase, Eo, was 11.6 mgL-. Figure 1, below, shows a Lineweaver-Burk plot for results obtained for the starch to dextrose enzymatic process. 0.13 0.12 0.11 0.10 Slope of plot 1.1 hr y-intercept of plot-0.033 hr L/g 0.09 0.08 0.07 0.04 0.05 0.06 0.07 0.08 0.09...
Most questions answered within 3 hours.
-
suppose you own a chain of five restaurants in
downtown Vancouver. as the manager, you want...
asked 3 minutes ago -
Here are summary statistics for randomly selected weights of
newborn girls:
nequals=225x overbarxequals=28.7hg, sequals=7.5hg. Construct a...
asked 6 minutes ago -
Q) Simplify the following functions and implement them with two-
level NAND gate circuits:
a) F(A,B,C,D)=...
asked 4 minutes ago -
If you could afford exactly 6 apples and 14 bananas, or 10
apples and 6 bananas,...
asked 19 minutes ago -
Write functions squareByValue,
squareByRef, squareByPointer that find the square of an integer, in
three different ways:...
asked 14 minutes ago -
Find the P - value for the test statistic ?=2.74z=2.74
for the following null and alternative...
asked 20 minutes ago -
An software company has three different promotion plans for
its software purchase:
plan A: each software...
asked 40 minutes ago -
If
P(A)=.62, P(B)=.47, & P(A or B)=.88. What is the likeliness of
selecting only A?
A)...
asked 39 minutes ago -
What is the FUTURE VALUE of $500 invested for 3 years at 7% with
ANNUAL Compounding...
asked 49 minutes ago -
Modify the method so that instead of manually making teams, it
reads it from a text...
asked 47 minutes ago -
1. Which of the following is not a principle to apply to
construction:
Select one:
a....
asked 49 minutes ago -
In what way is a Christian’s position made more challenging by
revealing faith in the workplace?...
asked 56 minutes ago