Homework Answers
![From the enzyme catalyst aqua relation. We have z B K CE.] cs.] kz=rate coust. [s.] tkm [6.] concentration - of enzyme = man](http://img.homeworklib.com/questions/4f9085e0-74a8-11ea-bed8-2978efcfd46d.png?x-oss-process=image/resize,w_560)
![In presence of inhibiton we have - Vmare [s] akutts] x = inhibitor constant x=1+ [I] from inverse plot we KI have ka = inhibi](http://img.homeworklib.com/questions/503b8ab0-74a8-11ea-b829-3f646b5085c5.png?x-oss-process=image/resize,w_560)
![Fon non-competitive inhibitor V- Vman (S.] km + & [so] % – km + x[s . Umare (so umanos km Vman Vmax v 1 um/umane as mane 1/[s](http://img.homeworklib.com/questions/50d74280-74a8-11ea-9213-b1315ea78f78.png?x-oss-process=image/resize,w_560)
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a) The technicians from the biochemistry lab have provided the following observed data for the rate...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
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...
A different experiment yields the following kinetic data Substrate] (mM)Vo (uM/min) no inhibitorVo (uM/min)+7 nM inhibitor...
A different experiment yields the following kinetic data Substrate] (mM)Vo (uM/min) no inhibitorVo (uM/min)+7 nM inhibitor 0.02 0.04 0.10 0.25 1.00 2.50 0.8 2.9 8.6 24 36 50 Plot the data for the kinetics of the enzyme (with and without the inhibitor) in a double reciprocal (Lineweaver-Burk) plot. Keep in mind that the x axis is 1/[S] and the y axis is 1/Vo. If you are using Excel you want to choose the (x,y) scatter plot (without a ne). You...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
2. Captopril was the first of a class of blood-pressure lowering drugs that work by reversibly...
2. Captopril was the first of a class of blood-pressure lowering drugs that work by reversibly inhibiting Angiotension-converting enzyme (ACE). Later to the market was Lisinopril. This class of drugs is the fifth most prescribed, approaching 200 million prescriptions per year in the US alone. ACE inhibitors work by preventing the proteolytic cleavage of angiotensin I by ACE to create its active form angiotensin II, which binds to receptors in the walls of blood vessels to initiate their relaxation, reducing...
A number of inhibitors for studyase have been found, the following data from enzyme assay analysis...
A number of inhibitors for studyase have been found, the following data from enzyme assay analysis has been determined: S (mM) Inhibitor A V(μmole/mL/sec) 1mL of 1mM used Inhibitor B V(μmole/mL/sec) 1mL of 3mM used Inhibitor C V(μmole/mL/sec) 1mL of 0.05mM used 1 4.3 5.5 5 2 8 9 8.69 4 14 13 13.7 8 21 16 19.6 12 26 18 22.2 Plot a Lineweaver-Burk plot of 1/V versus 1/S (on 1 graph) of each of the inhibitors. Determine...
Can someone please help with questions ii-vi? 6. Many types of cancerous tumors have cells with...
Can someone please help with questions ii-vi?
6. Many types of cancerous tumors have cells with a high dependence on glycolysis for generating the ATP needed for growth. Even in the presence of oxygen, these cells use glycolysis and lactate fermentation as their main source of ATP. i.) Give a balanced reaction for the reaction catalyzed by the enzyme lactate dehydrogenase (LDH). Give the structures of pyruvate and lactate, and add the names of any additional reactants or products needed...
3. Use the below tables to complete lab calculations on the worksheet on pages 2-6 of...
3. Use the below tables to complete lab calculations on the worksheet on pages 2-6 of this document. You will submit the worksheet via dropbox on Canvas by you assigned lab time the week of March 30th through April 3rd. A document with sample calculations of different concentrations is provided to you on canvas. Enzyme Kinetics Lab Buffer volume (mL) Enzyme Volume (ml) Substrate Volume (ml) TOTAL VOLUME (mL) 0.04 0.5 1.5 0.04 0.25 1.5 0.04 0.1 1.5 0.04 0.05...
Valganciclovir was synthesised from ganciclovir (1) using an esterase enzyme in an organic solvent giving two...
Valganciclovir was synthesised from ganciclovir (1) using an esterase enzyme in an organic solvent giving two isomers as shown in the scheme below: esterase enzyme in organic solvent NA NH HN HO ganciclovir N unwanted isomer During this reaction, inhibition of the esterase enzyme was observed and it was proposed that the cause of this was binding of the unwanted isomer (2). In order to test this hypothesis, 2 was added to the reaction mixture. The data obtained from these...
2. Using the data in the table, determine the rate constant of the reaction and select...
2. Using the data in the table, determine the rate constant of the reaction and select the appropriate units. A+2B⟶C+D Trial [A] (M)[A] (M) [B] (M)[B] (M) Rate (M/s) 1 0.340 0.340 0.0127 2 0.340 0.680 0.0127 3 0.680 0.340 0.0508 k= Units 3. The rate constant for this first‑order reaction is 0.480 s−1 at 400 ∘C. A⟶products How long, in seconds, would it take for the concentration of A to decrease from 0.650 M to 0.270 M? 4. After...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
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...
A different experiment yields the following kinetic data Substrate] (mM)Vo (uM/min) no inhibitorVo (uM/min)+7 nM inhibitor 0.02 0.04 0.10 0.25 1.00 2.50 0.8 2.9 8.6 24 36 50 Plot the data for the kinetics of the enzyme (with and without the inhibitor) in a double reciprocal (Lineweaver-Burk) plot. Keep in mind that the x axis is 1/[S] and the y axis is 1/Vo. If you are using Excel you want to choose the (x,y) scatter plot (without a ne). You...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
2. Captopril was the first of a class of blood-pressure lowering drugs that work by reversibly inhibiting Angiotension-converting enzyme (ACE). Later to the market was Lisinopril. This class of drugs is the fifth most prescribed, approaching 200 million prescriptions per year in the US alone. ACE inhibitors work by preventing the proteolytic cleavage of angiotensin I by ACE to create its active form angiotensin II, which binds to receptors in the walls of blood vessels to initiate their relaxation, reducing...
Can someone please help with questions ii-vi?
6. Many types of cancerous tumors have cells with a high dependence on glycolysis for generating the ATP needed for growth. Even in the presence of oxygen, these cells use glycolysis and lactate fermentation as their main source of ATP. i.) Give a balanced reaction for the reaction catalyzed by the enzyme lactate dehydrogenase (LDH). Give the structures of pyruvate and lactate, and add the names of any additional reactants or products needed...
3. Use the below tables to complete lab calculations on the worksheet on pages 2-6 of this document. You will submit the worksheet via dropbox on Canvas by you assigned lab time the week of March 30th through April 3rd. A document with sample calculations of different concentrations is provided to you on canvas. Enzyme Kinetics Lab Buffer volume (mL) Enzyme Volume (ml) Substrate Volume (ml) TOTAL VOLUME (mL) 0.04 0.5 1.5 0.04 0.25 1.5 0.04 0.1 1.5 0.04 0.05...
Valganciclovir was synthesised from ganciclovir (1) using an esterase enzyme in an organic solvent giving two isomers as shown in the scheme below: esterase enzyme in organic solvent NA NH HN HO ganciclovir N unwanted isomer During this reaction, inhibition of the esterase enzyme was observed and it was proposed that the cause of this was binding of the unwanted isomer (2). In order to test this hypothesis, 2 was added to the reaction mixture. The data obtained from these...
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