Question
In: Chemistry
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 nM of the enzyme X is used in the experiment, what will be the Vmax and Km values of the enzyme X?
Solutions
queen_honey_blossom answered 7 months agoRelated Solutions
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...
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...
An experimenter performs two sets of enzyme kinetics experiments. One set of experiments, when plotted as...
An experimenter performs two sets of enzyme kinetics
experiments. One set of experiments, when plotted as a
double-reciprocal plot, yielded a y-intercept of 0.043
μM-1·min and an x-intercept of -20.0 mM-1. A second set of
experiments, when similarly plotted, yielded a y-intercept
of 0.129 μM-1·min and an x-intercept of -60.0 mM-1. The
second set of experiments contained 92 nM of an uncompetitive
inhibitor. Given these data, what is the Ki' (in nM to the
nearest tenths) for this inhibitor? Hint:...
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...
1. The following data were obtained from 3 separate enzyme kinetic experiments using 3 different substrates...
1. The following data were obtained from 3 separate
enzyme kinetic experiments using 3 different substrates S1, S2 and
S3 forming products P1, P2 and P3 respectively. The amount of
enzyme in each reaction is 1 µM. Find out the rate and graph the
data using a Michaelis-Menton and Lineweaver-Burk plots and
determine the values for Km, Vmax, Kcat, and Kcat/Km. Which among
the 3 substrate is best substrate for this enzyme and why? (4
points)
[S] (mM) [P1] (mM)...
You are studying the kinetics of the reaction: &nb
You are studying the kinetics of the reaction:
H2(g) + F2(g) → 2HF(g)
You are attempting to determine a mechanism for the reaction.
You run 2 separate reaction trials keeping one reactant at a much
higher pressure than the other reactant. The lower pressure
reactant begins at 1.000 atm. OOPS! You forget to record which
reactant was at the higher pressure. The data you collected for the
first trial are:
Pressure of
HF(atm)
Time(min)
0
0
0.300
30.0
0.600 ...
In Enzyme kinetics can someone explain how color develops by explaining the chemical reaction that occurs...
In Enzyme kinetics can someone explain how color develops by
explaining the chemical reaction that occurs with BAPNA.
also Draw the structure of benzamidine and comment on the type
of inhibitor that benzamidine is and how this relates to its
structure.
3) In enzyme kinetics why does the initial reaction rate (vo) resemble the steady state in...
3) In enzyme kinetics why does the initial reaction
rate (vo) resemble the steady state in living
cells?
4) Also, in enzyme kinetics the Km value is an
indicator of enzyme binding efficiency, is a low or high Km value
indicative of better efficiency in living cells? Why?
5) Consider competitive inhibitors. Why does their
presence raise the Km value?
You are studying the kinetics of the reaction: (this is due tomorrow!!) ...
You are studying the kinetics of the reaction: (this is due
tomorrow!!)
H2(g) + F2(g) → 2HF(g)
You are attempting to determine a mechanism for the reaction.
You run 2 separate reaction trials keeping one reactant at a much
higher pressure than the other reactant. The lower pressure
reactant begins at 1.000 atm. OOPS! You forget to record which
reactant was at the higher pressure. The data you collected for the
first trial are:
Pressure of...
An enzyme catalyzed reaction has a Km of 3.76 mM and a Vmax of 6.72 nM/s....
An enzyme catalyzed reaction has a Km of 3.76 mM and a Vmax of
6.72 nM/s. What is the reaction velocity in nM/s,
when the substrate concentrations are:
A. 0.500 mM
B. 15.6 mM
C. 252 mM
D. Now assume you have added a competitive inhibitor that has a
concentration of 15.6 µM with a KI of 7.30 µM to the
enzyme in question 9. Calculate the velocity at the same substrate
concentrations as above:
E. 0.500 mM
F. 15.6...
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