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.
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...
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...
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...
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.
1. If the enzyme-catalyzed reaction E + S ↔ ES ↔ E + P takes
place near Vmax to the enzyme (E), what can be concluded about the
relative concentrations of S and ES?
a) High [S], [ES] is low
b) High [S], [ES] are at their maximum
c) Low [S], [ES] is low
d) Low [S], [ES] is at its maximum
2. Which of the following statements about Michaelis-Menten
kinetics is correct?
a) Km = the substrate concentration required...
1.
Starting from the enzyme-catalyzed reaction:
S -> P
Derive the (a) Michaelis-Menten Equation (b) starting from the
Michaelis-Menten equation, derive the Lineweaver-Burker plot.
Provide brief explanation in each step.
2. Predict the optimum pH and temperature for human saliat
amylase. Why did you arrive on the prediction?
A jet of water 50 mm in diameter with a velocity of 20 m/s
strikes a flat plate inclined at an angle of 30° to the axis of the
jet. Determine
(i) the normal force exerted on the plate when the plate is
stationary
(ii) the normal force exerted on the plate when the plate is
moving at 5 m/s in the direction of the jet
(iii) the work-done on the plate and the efficiency for case
(ii).
For the reaction 2NO_2 (g)→2NO_2 (g)+O_2 (g)
The data given below was
collected:
Time(s)
[NO2]
Ln[NO2]
1/[NO2]
0
0.110
-2.205
9.066
1
0.108
-2.229
9.294
2
0.105
-2.254
9.524
3
0.103
-2.277
9.747
Obtain the average rate of decomposition of NO_2 in units of M/s
for each interval.
What is the order of the reaction with respect to NO_2?
How long would it take for the concentration to decrease to
.0900M?
The data presented below were collected on the amount of time,
in hours; it takes an employee, to process an order at a local
plumbing wholesaler.
2.8
4.9
0.5
13.2
14.2
8.9
3.7
15.2
11.2
13.4
5.5
10.2
1.1
14.2
7.8
4.5
10.9
8.8
18.2
17.1
Construct a stem-and-leaf display of the data.
Construct a frequency distribution of the data
Construct cumulative frequency and cumulative percent
distributions of the data
Construct a frequency histogram of the data.
Determine the percentage...