Question
In: Chemistry
The value of Km for the shown data for a hexokinase-catalyzed reaction is [Blank] with the...
The value of Km for the shown data for a hexokinase-catalyzed reaction is [Blank] with the unit of [Blank] The value of Vmax for the same reaction is [Blank] with the unit of [Blank] Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (μM, 1/μM, μM/second, μM x second, mM, 1/mM, second, 1/second, mM/second, mM x second)
|
Glucose concentration (mM) |
ν0 (mM/sec) |
|
0.10 0.20 0.40 0.80 1.6 |
0.34 0.53 0.74 0.91 1.0 |
Solutions
queen_honey_blossom answered 2 years agoRelated Solutions
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...
The following reaction rate data are collected upon analysis of an enzyme catalyzed hydrolysis. The reaction...
The following reaction rate data are collected upon analysis of
an enzyme catalyzed hydrolysis. The reaction is carried out with
two different inhibitors. Determine the modes of inhibition for each
inhibitor. (The rates provided are relative to the rate measured in
the absence of inhibitor. The enzyme concentration for each set of
data is equal.)
No inhibitor
[S]0 (10−2 M) 1.25 3.84 5.81 7.13
v0 0.398 0.669 0.859 1.000
[I1]– –2mmol/L
[S]0 (10−2 M) 1.25 2.5 4.00 5.50
v0 0.179...
Consider the following data for an enzyme catalyzed hydrolysis reaction in the presence and absence of...
Consider the following data for an enzyme catalyzed hydrolysis
reaction in the presence and absence of inhibitor I:
[Substrate]
M
vo
(µmol/min)
voI (µmol/min)
6x10-6 20.8 4.2
1x10-5
29
5.8
2x10-5
45
9
6x10-5
67.6
13.6
1.8x10-4
87
16.2
Use the above data, do the following:
a. Generate Lineweaver-Burk plots of the data.
b. Explain the significance of the x-interecpt, y-intercept, and
the slope.
c. Identify the type of inhibition.
How do the Km values of glucokinase and hexokinase reflect their roles in sugar metabolism ?
How do the Km values of glucokinase and hexokinase reflect their
roles in sugar metabolism ?
The data to the below were collected for the bovine carbonic anhydrase-catalyzed reaction described by CO2...
The data to the below were collected for the bovine carbonic
anhydrase-catalyzed reaction described by
CO2 (aq) + H2O (l) -->H+ (aq) + HCO3- (aq)
[CO2] (mmol * L^-1)
R (ݵmol * L^-1 * s^-1)
1.25
28.74
2.50
48.61
5.00
80.28
20.00
155.59
Use these values to determine the value of KM, the
Michaelis-Menten constant. Answer the four parts below.
a) If you were to plot this data to graphically determine Rmax
and KM using a Lineweaver-Burk plot, what would...
Imagine that you are observing an enzyme-catalyzed reaction in the laboratory. The reaction is progressing as...
Imagine that you are observing an enzyme-catalyzed reaction in
the laboratory. The reaction is progressing as expected. As you
periodically add more enzyme, the reaction increases proportionally
until suddenly it stops increasing. At this point, no matter how
much more enzyme that you add, the reaction rate does not change.
Assuming no other chemicals have been added or changed, explain why
the reaction rate has leveled off.
A.) Let’s assume that the hexokinase reaction proceeds in the following manner as opposed to what...
A.) Let’s assume that the hexokinase reaction proceeds in the
following manner as opposed to what we see in A) and B). Given this
what is the new Keq?
fructose-6-phosphate + ATP ↔ F16BP + ADP deltaG° = -14.2
kJ/mol
B.) If we assume that the [ATP] is 10x greater than the [ADP]
what is the new molar ratio of [F16BP]:[fructose-6-phosphate] at
equilibrium?
C.) If the cellular concentrations of fructose-6-phosphate and
F16BP are 0.028mM and 0.014 mM respectively what does...
What is the difference between a a reaction that is catalyzed by a kinase compared to...
What is the difference between a a reaction that is catalyzed by
a kinase compared to one that is catalyzed by a phosphorylase?
(Describe the various roles/mechanisms of each, utilization of ATP,
etc).
What is the value for Ecell for the reaction shown below if each one of the...
What is the value for Ecell for the reaction shown below if each
one of the dissolved species has a concentration of 0.1 M?
2 Fe3+ (aq) + 2 I-(aq) → 2 Fe2+(aq) + I2(s)
a) -0.35 V
b) -0.29 V
c) +0.11 V
d) +0.17 V
The data below were collected for an enzyme-catalyzed reaction. [S] (mM) 0.25 0.50 1.00 2.00 V0...
The data below were collected for an enzyme-catalyzed
reaction.
[S] (mM)
0.25
0.50
1.00
2.00
V0 (mM*s-1)
2.00
3.33
5.00
6.67
Determine Vmax and Km for this reaction.
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