The next 3 questions are related. The results of an enzyme analysis are: KM=1.1x10-5 M; VMAX=47.6...
The next 3 questions are related. The results of an enzyme
analysis are: KM=1.1x10-5
M; VMAX=47.6 μM/min. What is the Lineweaver Burk plot
equation (recall: y=1/Keq and x=1/[S])?
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The next 3 questions are related. The results of an enzyme
analysis are: KM=1.1x10-5
M; VMAX=47.6...
An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of product/minute/µg...
An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of product/minute/µg of enzyme. After exposure to an inhibitor and analysis on a Lineweaver - Burk plot the following values are obtained: -1/KM = - 0.05 liters/µmole and 1/Vmax = 0.04 (mmoles of product/minute/µg of enzyme)-1. What kind of inhibitor was used in the experiment?
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round the answer to the 3 significant figures) 0.7 0.6 0.5 y =0.4843x+0.1951 0.4 1/v (pmol/L)/min) 0.3 30.2 0.1 0 0 0.1 0.2 0.3 0.5 0.6 0.7 0.8 0.9 0.4 1/[S] (umol/L) 2.50M 2.50 M 2.48 M 248M
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
i need help with all question 5 please! thank you Question 5: Use the data below...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]....
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The...
Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (uM) vo (mg /min) vo (mg /min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 5.0 50.8 14.6 10 72...
The results for enzyme activity analysis are presented in Table 5 (below). In this case, do...
The results for enzyme activity analysis are presented in Table 5 (below). In this case, do not use the graph to determine: (1.5 pts each) (Hint- use M-M equation) a) Vmax; b) Km; c) initial velocity at [S] 1 x 10-1 M; d) the amount of product formed during the first 5 minutes at [S] 2x10 3M; at a [S of 2x10 6M? e) what is Km and Vmax if the free [E is increased 3-fold? 3. v (umol/min 0.25...
1. an enzyme is observed to approach an initial velocity of 0.1M/s as more and more...
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round the answer to the 3 significant figures) 0.7 0.6 0.5 y =0.4843x+0.1951 0.4 1/v (pmol/L)/min) 0.3 30.2 0.1 0 0 0.1 0.2 0.3 0.5 0.6 0.7 0.8 0.9 0.4 1/[S] (umol/L) 2.50M 2.50 M 2.48 M 248M
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
The results for enzyme activity analysis are presented in Table 5 (below). In this case, do not use the graph to determine: (1.5 pts each) (Hint- use M-M equation) a) Vmax; b) Km; c) initial velocity at [S] 1 x 10-1 M; d) the amount of product formed during the first 5 minutes at [S] 2x10 3M; at a [S of 2x10 6M? e) what is Km and Vmax if the free [E is increased 3-fold? 3. v (umol/min 0.25...
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
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