how different types of inhibitions affect Vmax and Km values, and illustrate the changes using double-reciprocal...
how different types of inhibitions affect Vmax and Km values, and illustrate the changes using double-reciprocal plots?
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how different types of inhibitions affect Vmax and Km values,
and illustrate the changes using double-reciprocal...
describe in details how different types of inhibitions affect Vmax and Km values, and illustrate the...
describe in details how different types of inhibitions affect Vmax and Km values, and illustrate the changes using double-reciprocal plots.
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each...
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each plot, demonstrating how Km and Vmax can be determined. On the same graphs, draw another plot where the same enzyme-catalyzed reaction is subjected to inhibition by a competitive inhibitor.
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
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]...
How do competitive inhibitors affect the KM and Vmax of an enzyme? Draw a plot of...
How do competitive inhibitors affect the KM and Vmax of an enzyme? Draw a plot of velocity as a function of substrate concentration, both with and without inhibitor added.
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
5.How would you determine the values of KM and Vmax from a: a) Michaelis-Menten plot b)...
5.How would you determine the values of KM and Vmax from a: a) Michaelis-Menten plot b) Lineweaver-Burke plot 6. How is general acid/base catalysis different from regular acid/base catalysis? 7. How would you recognize the process of covalent catalysis in an enzyme reaction mechanism?
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using...
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x...
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x + 3. Calculate Vmax (mmol/s) and Km (mmol/L). b. [5 points] Estimate V for caffeine concentration of 400 mmol/L. c. [10 points] The enzyme caffeine dehydrogenase (Cdh) is an inducible quinone-dependent oxidoreductase. Describe how the addition of caffeine into the culture medium will be detected and transcriptionally regulated by the two-component system in Pseudomonas sp. CBB1.
Nobody has been able to solve the Km. The Vmax values are correct. I believe I...
Nobody has been able to solve the Km. The Vmax values are
correct. I believe I have my graph wrong. Can someone please help
me solve this.
Using the Lineweaver-Burk Equation 1/Vo Km/Vmax[S]1/Vmax) create a graph of both the Non-Inhibited data and Inhibited data below (on the same graph axes) and calculate the KM and VMax for each line. Vo (umol/L.min) Vo (Hmol/L-min) [Sol (umol/L) Non-Inhibited Data Inhibited Data .00e-06 13.9 7.60 .00e-06 18.0 9.90 ..10e- 05 10e-05 26.0 14.8...
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]...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
Nobody has been able to solve the Km. The Vmax values are
correct. I believe I have my graph wrong. Can someone please help
me solve this.
Using the Lineweaver-Burk Equation 1/Vo Km/Vmax[S]1/Vmax) create a graph of both the Non-Inhibited data and Inhibited data below (on the same graph axes) and calculate the KM and VMax for each line. Vo (umol/L.min) Vo (Hmol/L-min) [Sol (umol/L) Non-Inhibited Data Inhibited Data .00e-06 13.9 7.60 .00e-06 18.0 9.90 ..10e- 05 10e-05 26.0 14.8...
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