Question
In: Chemistry
An enzyme was obtained in Dr. Cai’s lab. To study the kinetics of this enzyme, a...
An enzyme was obtained in Dr. Cai’s lab. To study the kinetics of this enzyme, a
graduate student measured the velocity of the reaction at a substrate concentration
of 0.2 mM substrate. He found the initial rate decreased to 1/3 after 1.2 mM
competitive inhibitor was added. KI, the dissociation constant for the inhibitor
binding to the enzyme, is 0.5 mM. What is the KM, the Michaelis constant?
A. 0.33 mM
B. 0.5 mM
C. 0.1 mM
D. 1 mM
E. 10 mM
Solutions
queen_honey_blossom answered 2 years agoRelated Solutions
1.The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics:...
1.The following data were obtained in a study of an enzyme known
to follow Michaelis-Menten kinetics:
2/27/ 20
V0 (mol/min)
217
325
433
488
647
Substrate added (mmol/L)
0.8 2 4 6 1,000
The Km for
A) 1 mM., B) 1000mM, C) 2mM, D ) 4mM, E) 6mM
this enzyme is approximately:
2. To
A) the enzyme concentration.
B) the initial velocity of the catalyzed reaction at [S]
>> Km.
C) the initial velocity of the catalyzed reaction at...
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you obtained the reaction rates at...
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you
obtained the reaction rates at different concentrations of
substrate (shown in the following table). Assume that the enzyme X
follows a typical Michaelis-Menten kinetics.
[substrate] (μM) Reaction rate (μmol/min)
2 7
5 17
10 29
20 44
50 67
100 80
200 89
500 95
1000 98
a) Estimate the Vmax and Km values of the enzyme in this
reaction using double reciprocal plot.
b) If 5.0 nM of...
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you obtained the reaction rates at...
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you
obtained the reaction rates at different concentrations of
substrate (shown in the following table). Assume that the enzyme X
follows a typical Michaelis-Menten kinetics.
[substrate] (μM) Reaction rate (μmol/s)
2 7
5 17
10 29
20 44
50 67
100 80
200 89
500 95
1000 98
a) Estimate the Vmax and Km values of the enzyme X in this
reaction using the double reciprocal plot.
b) If 5.0...
3. The kinetics of an enzyme are studied in the absence and presence of an inhibitor...
3. The kinetics of an enzyme are studied in the absence and
presence of an inhibitor (A). The intial rate is given as a
function of substrat concentration in the table.
V0
V0
[S] (mmol/L)
no Inhibitor
Inhibitor A
1.25
1.72
0.98
1.67
2.04
1.17
2.5
2.63
1.47
5.00
3.33
1.96
10.00
4.17
2.38
(a) What kind oof competitor is inhibition is involved
(competitive, noncompetitive, uncompetitive)? [Please Provide
Graph]
(b) Determine Vmax and Km in the absence and presence of...
Question 1: Dr. Snow replicated the previous study and obtained scores for the three samples listed...
Question 1:
Dr. Snow replicated the previous study
and obtained scores for the three samples listed in the
table below:
Low HS
Medium HS
High HS
4
14
17
9
12
12
6
3
13
8
26
15
14
15
18
16
19
16
8
17
16
10
5
14
In SPSS, analyze the data Dr. Snow collected using a one-way
ANOVA.
Complete the table below using the results found in the output
box labeled Descriptives, then use the response...
In your lab you are studying the kinetics of the degradation of a pain killer in...
In your lab you are studying the kinetics of the degradation of
a pain killer in the human liver. You are monitoring the
concentration of the pain killer over a period of time. The initial
concentration of the pain killer in your experiment was 1.51 M.
After 15.58 hours the concentration was found to be 0.7550 M. In
another 15.58 hours the concentration was found to be 0.3775 M (t =
31.16 hours overall).
If another experiment were set up...
What assumption concerning substrate concentration is made in the discussion of enzyme kinetics? Why is this...
What assumption concerning substrate concentration is
made in the discussion of enzyme kinetics? Why is this
important?
In Michaelis-Menten kinetics, what values would make an enzyme “good” at catalysis?
In Michaelis-Menten kinetics, what values would make an enzyme
“good” at catalysis?
What are the key differences between the Michaelis-Menten model that describes enzyme kinetics and the Monod...
What are the key differences between the Michaelis-Menten model
that describes enzyme kinetics and the Monod model that describes
whole-cell or community kinetics?
Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table....
Initial rate data for an enzyme that obeys Michaelis-Menten
kinetics are shown in the following table. When the enzyme
concentration is 3 nmol ml−1, a Lineweaver-Burk plot of this data
gives a line with a y-intercept of 0.00426
(μmol−1ml s).
[S] μM
v0 (μmol ml−1 s−1)
320
169
160
132
80.0
92.0
40.0
57.2
20.0
32.6
10.0
17.5
a. Calculate Kcat for the reaction
b. Calculate Km for the enzyme
cWhen the reactions in part (B) are repeated in the...
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