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Enzymes can be inhibited by binding to various molecules. These inhibitors can affect the reaction rate (Vmax) and/or Km, the concentration of substrate which permits the enzyme to achieve half Vmax.
Enzymes can be inhibited by binding to various molecules. These inhibitors can affect the reaction rate (Vmax) and/or Km, the concentration of substrate which permits the enzyme to achieve half Vmax.
There are three classes of enzyme inhibitors:
There are three classes of enzyme inhibitors:
Competitive: Increases Km
Competitive: Increases Km
Non-Competitive: Decreases Vmax
Non-Competitive: Decreases Vmax
Uncompetitive: Decreases Km and Vmax
Uncompetitive: Decreases Km and Vmax
Use the data provided below for inhibition of Enzyme 1 to plot a Lineweaver-Burk Plot (1/substrate amount vs 1/product). Use your graphs to determine the type of inhibition that is occurring for each inhibitor (A and B).
Use the data provided below for inhibition of Enzyme 1 to plot a Lineweaver-Burk Plot (1/substrate amount vs 1/product). Use your graphs to determine the type of inhibition that is occurring for each inhibitor (A and B).
Reaction Conditions
Reaction Conditions
The following substrate concentrations were tested for each set of experiments
The following substrate concentrations were tested for each set of experiments
0 mM
25 mM
50 mM
75 mM
100 mM
125 mM
150 mM
175 mM
200 mM
225 mM
250 mM
Shown below are the Incubation Conditions that were used
Shown below are the Incubation Conditions that were used
pH Optimal pH for Enzyme 1
Amount of Enzyme 100 ul
Incubation Time 10 minutes
Temperature Optimal Temperature for Enzyme 1
Enzyme Selection
Enzyme Selection
Select an Inhibitor to see the Effects on Enzyme 1. These results are also shown in graphical form at the bottom of the page.
Select an Inhibitor to see the Effects on Enzyme 1. These results are also shown in graphical form at the bottom of the page.
Inhibitor A
Inhibitor A
substrate (mM) No Inhibitor 125 mM 250 mM 500 mM 1000 mM
0 0 0.01 0.01 0.01 0.03
25 22.92 21.5 19.4 16.92 12.81
50 41.33 36.56 33.55 28.77 22.87
75 49.98 46.63 42.75 37.74 30.67
100 55.89 52.08 49.12 43.79 36.64
125 60.09 56.79 53.83 47.98 40.61
150 62.55 58.66 55.4 51.23 43.48
175 64.07 60.65 59.36 54.94 46.94
200 65.23 63.37 58.93 56.83 50.59
225 65.53 64.75 62.14 58.33 51.74
250 66.67 63.89 64.19 59.25 52.75
Inhibitor B
Inhibitor B
substrate (mM) No Inhibitor 12.5 mM 25 mM 50 mM 100 mM
0 0.03 0.03 0.03 0.02 0.02
25 22.72 18.91 16.13 11.39 7.29
50 40.54 29.66 23.39 16.29 9.89
75 50.29 35.15 27.01 18.41 10.92
100 56.69 38.79 28.89 19.54 11.68
125 60.33 39.96 30.14 20.59 11.89
150 61.87 41.85 30.69 20.33 12.42
175 63.17 42.8 32.27 20.77 12.42
200 65.24 42.59 32.22 21.5 12.56
225 64.89 43.43 32.55 21.81 13.2
250 67.02 43.79 33.68 21.61 13.17
Graphs showing the effects of Inhibitor A and Inhibitor B on the activity of Enzyme 1 are shown below.
Graphs showing the effects of Inhibitor A and Inhibitor B on the activity of Enzyme 1 are shown below.
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