Find Km, Vmax, Ki and Kcat values.
Find Vmax, Km and Ki values according to the graph
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Find Km, Vmax, Ki and Kcat values.
Find Vmax, Km and Ki values according to the...
)* (Vmax). 4. When [S] = KM, Vo=( A) 0.5 B) KM C) 0.75 D) kcat...
)* (Vmax). 4. When [S] = KM, Vo=( A) 0.5 B) KM C) 0.75 D) kcat E) [S] 5. The overall transformation shown in the following reaction: E s. Es p + E For the reaction, the steady state assumption A) ES breakdown occurs at the same rate as ES formation B) [P]>>[E] C) implies that ki-k-1 D) implies that k., and k2 are such that the [ES] = k1[ES] E) [S] = [P]
2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km...
2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km O y=7x+2.5 for enzyme A (in mM and s). b. Suppose you want to compare similar enzymes A (above Kcat=500) with enzyme B (Km=2.0, Kcat=450) to find out which enzyme has a higher catalytic efficiency; which enzyme has the higher catalytic efficiency?
Kcat =30.0 s-1 Km= 0.005 M Operating at 1/4 Vmax What is [S] ? The solutions...
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
a. what are the values of Vmax and Km in the abscence if the inhibitor what...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where...
Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where [S]=6mM, it was found that Vo=480nM/min. What was the enzyme concentration? Give your answer in nM. Using the same kcat and Km as the previous question, if [Et]=0.5uM gives a Vo=5 uM/min, what wat the [S]? Give your answer in uM. reaction is run with the kcat=20/min and the Km=4uM. Use the enzyme concentration from question 1 above. A very strong inhibitor is added creating...
Michaelis GRAPH 4 3.5 3 2.5 Vo (unit/min) 2 1.5 1 0.5 0 0 50 100...
Michaelis GRAPH 4 3.5 3 2.5 Vo (unit/min) 2 1.5 1 0.5 0 0 50 100 200 250 300 150 [H4] (mm) Q7: Using the plotted “Michaelis Graph", you will provide an approximate value for both the Vmax and the Km for this SGRGK short peptide. Do not forget the units for these two parameters. To secure full credit, you must provide clear explanations on how you determined these two Vmax and Km (15pts).
Time (s) NO2] ILKIO 1.00E-02 60 6.83E-03 as 120 5.18E-03 180 4.18E-03 oaibrate tdn 240 3.50E-03...
Time (s) NO2] ILKIO 1.00E-02 60 6.83E-03 as 120 5.18E-03 180 4.18E-03 oaibrate tdn 240 3.50E-03 300 3.01E-03 otoge 360 2.64E-03 2. From the graphs and the R2 values, what is the order of the reaction? 3. The balanced chemical reaction for the degradation of NO2 into NO and O2 is: 2 NO22 NO + O2 The rate law for the reaction is: Rate = k[NO22 If the instantaneous rate at 60 seconds is 0.361 M/s, what is the value...
An enzyme has a Km for substrate of 10 mM and Vmax of 5 mol L-1...
An enzyme has a Km for substrate of 10 mM and Vmax of 5 mol L-1 sec-1 at a total enzyme concentration of 1 nM. At [S] = 10 mM, kcat is: A) 2500 per M per sec. B) 5000 per M per sec. C) 1250 per M per sec. D) 2500 per sec. E) 5000 per sec.
The confirmatory method of identifying illegal drugs is GC-MS. The suspected drug is analyzed and...
The confirmatory method of identifying illegal drugs is GC-MS.
The suspected drug is analyzed and its spectrum is compared to a
library of spectra. Using the following spectra, is it possible to
identify the evidence sample? Justify either a positive or negative
finding.
Evidence 100 80 60 40 20 0 0 50 100 150 200 250 300 350 400 w/s Morphine 100 80 e0 40 20 LSD 100 80 S 40 3 20 д 50 100 150 200 250 300...
)* (Vmax). 4. When [S] = KM, Vo=( A) 0.5 B) KM C) 0.75 D) kcat E) [S] 5. The overall transformation shown in the following reaction: E s. Es p + E For the reaction, the steady state assumption A) ES breakdown occurs at the same rate as ES formation B) [P]>>[E] C) implies that ki-k-1 D) implies that k., and k2 are such that the [ES] = k1[ES] E) [S] = [P]
2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km O y=7x+2.5 for enzyme A (in mM and s). b. Suppose you want to compare similar enzymes A (above Kcat=500) with enzyme B (Km=2.0, Kcat=450) to find out which enzyme has a higher catalytic efficiency; which enzyme has the higher catalytic efficiency?
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
Michaelis GRAPH 4 3.5 3 2.5 Vo (unit/min) 2 1.5 1 0.5 0 0 50 100 200 250 300 150 [H4] (mm) Q7: Using the plotted “Michaelis Graph", you will provide an approximate value for both the Vmax and the Km for this SGRGK short peptide. Do not forget the units for these two parameters. To secure full credit, you must provide clear explanations on how you determined these two Vmax and Km (15pts).
Time (s) NO2] ILKIO 1.00E-02 60 6.83E-03 as 120 5.18E-03 180 4.18E-03 oaibrate tdn 240 3.50E-03 300 3.01E-03 otoge 360 2.64E-03 2. From the graphs and the R2 values, what is the order of the reaction? 3. The balanced chemical reaction for the degradation of NO2 into NO and O2 is: 2 NO22 NO + O2 The rate law for the reaction is: Rate = k[NO22 If the instantaneous rate at 60 seconds is 0.361 M/s, what is the value...
The confirmatory method of identifying illegal drugs is GC-MS.
The suspected drug is analyzed and its spectrum is compared to a
library of spectra. Using the following spectra, is it possible to
identify the evidence sample? Justify either a positive or negative
finding.
Evidence 100 80 60 40 20 0 0 50 100 150 200 250 300 350 400 w/s Morphine 100 80 e0 40 20 LSD 100 80 S 40 3 20 д 50 100 150 200 250 300...
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