Question

In: Chemistry

The enzyme is studied in the presence of a different inhibitor (inhibitor B). In this case,...

The enzyme is studied in the presence of a different inhibitor (inhibitor B). In this case, two different concentrations of inhibitor are used. Data are as follows:

a) Determine the apparent Vmax at each inhibitor concentration.

b) Determine the apparent KM at each inhibitor concentration.

c) Estimate KI from these data. [Hint: Calculate the K_I at 3 mM and at 5 mM; and then take the average of the two K_Ivalues.]

v[(mmol/L)min−1]
[S](mmol/L)	No inhibitor	3 mM inhibitor B	5 mM inhibitor B
1.25	1.72	1.25	1.01
1.67	2.04	1.54	1.26
2.50	2.63	2.00	1.72
5.00	3.33	2.86	2.56
10.00	4.17	3.70	3.49

Expert Solution

queen_honey_blossom answered 2 years ago

3. The kinetics of an enzyme are studied in the absence and presence of an inhibitor...

3. The kinetics of an enzyme are studied in the absence and presence of an inhibitor (A). The intial rate is given as a function of substrat concentration in the table. V0 V0 [S] (mmol/L) no Inhibitor Inhibitor A 1.25 1.72 0.98 1.67 2.04 1.17 2.5 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 (a) What kind oof competitor is inhibition is involved (competitive, noncompetitive, uncompetitive)? [Please Provide Graph] (b) Determine Vmax and Km in the absence and presence of...

Students collected Beta-fructosidase enzyme activity data in the presence and absence of an unknown inhibitor. P-nitrophenol...

Students collected Beta-fructosidase enzyme activity data in the presence and absence of an unknown inhibitor. P-nitrophenol was used as a read out for enzyme activity. Quantity of product was determined from the absorbance of each sample after 5 minutes of reaction. Using the information, complete the table below and create a properly labeled Lineweaver burke plot with the appropriate axes and best fit lines for the data, in excel (graph is worth 6pts). Using this plot, calculate the approximate Vmax...

Below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibitor.

Below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibitor. Part A Indicate what type of inhibition is predicted based on Lineweaver-Burk plot. mixed inhibition competitive inhibition uncompetitive inhibition Part B Indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. red - without inhibitor, blue - with inhibitor blue - without inhibitor, red - with inhibitor Part C...

Explain the extrinsic regulation of GFR. Explain how an angiotensin converting enzyme inhibitor (ACE inhibitor) such...

Explain the extrinsic regulation of GFR. Explain how an angiotensin converting enzyme inhibitor (ACE inhibitor) such as captopril would be effective as an antihypertensive.nnn

The effect of an inhibitor on an enzyme was tested and the experiment gave the results...

The effect of an inhibitor on an enzyme was tested and the experiment gave the results below. Plot on Excel the data using a double-reciprocal plot (Lineweaver-Burke), determine Km and Vmax of the no inhibitor and each type of inhibitor and the type of inhibition that is occurring. [S] µM V (µmol/min) V (µmol/min) V (µmol/min) with 0.0 nM with 25 nM with 50 nM Inhibitor Inhibitor Inhibitor ______ ___________ ___________ ___________ 0.4 0.22 0.21 0.20...

The following kinetic data were obtained for an enzyme in the absence of inhibitor (1)

Enzymes Kinetics:The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Etotal] is the same in each experiment. [S](mM) 1 ν(μmol/mL. sec) 2 ν(μmol/mL. sec) 3 ν(μmol/mL. sec) 1 12 4.3 5.5 2 20 8 9 4 29 14 13 5 35 21 16 12 40 26 18 a. From a double-reciprocal plot of the data, Determine Vmax...

How does a competitive inhibitor change the Km and Vmax values for an enzyme such as...

How does a competitive inhibitor change the Km and Vmax values for an enzyme such as Penicillin?

Determine the Vmax and the Km of the enzyme in the absence and presence of each...

Determine the Vmax and the Km of the enzyme in the absence and presence of each inhibitor. Calculate the KI for each inhibitor. Are the inhibitors all the same? Which is the best inhibitor and why? What is the catalytic efficiency and turnover number of the enzyme knowing that during the experiments its concentration was 2 nM? What happens to the catalytic efficiency and turnover number of the enzyme in the presence of each of the inhibitor? The following velocity...

How does a suicide inhibitor and transition state analogues work on an enzyme? Could they be...

How does a suicide inhibitor and transition state analogues work on an enzyme? Could they be used in developing pharmaceuticals?

1. Why does a noncompetitive inhibitor decrease the Vmax of an enzyme? 2. The insertion of...

1. Why does a noncompetitive inhibitor decrease the Vmax of an enzyme? 2. The insertion of cholesterol into the lipid bilayer does what to the bilayer?