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Magazine Chapter 12: Q19P (page 399)
Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor.
[S] (mM) | v鈧� (mM min鈦宦�) | v鈧� with I present (mM min鈦宦�) |
1 | 1.3 | 0.8 |
2 | 2.0 | 1.2 |
4 | 2.8 | 1.7 |
8 | 3.6 | 2.2 |
12 | 4.0 | 2.4 |
Short Answer
The inhibitor is a mixed inhibitor.
Step by step solution
Biological protein catalysts
Enzymes are biological protein catalysts that change the rate of a process in a living organism. The molecule that binds to the enzyme's substrate binding site is referred to as the substrate. Enzyme inhibitors stop enzymes from functioning.
Inhibition of an enzymatic reaction
Both free enzyme and enzyme-substrate complexes bind to mixed inhibitors. The following data is used to create a Lineweaver-Burk graph. Extrapolation is carried out on the acquired lines.
A factor was added to theMichaelis-Menton equation. 鈭� is a function of the concentration of a competitive inhibitor and the inhibitor's affinity for the enzyme. The concentration of an uncompetitive inhibitor and the inhibitor's affinity for the enzyme is used to calculate 鈭澦�. If there is an inhibitor, 鈭� and 鈭澦� cannot be smaller than 1. Both with and without inhibitor are displayed on the graph. To the left of the 1/v axis, the lines cross.
Tabulation for plotting the graph
1/[S] (mM) | 1/v鈧� (mM min鈦宦�) | 1/v鈧� with I present (mM min鈦宦�) |
1.0 | 0.7 | 1.2 |
0.5 | 0.5 | 0.8 |
0.3 | 0.4 | 0.6 |
0.1 | 0.3 | 0.5 |
0.08 | 0.2 | 0.4 |
Graphical representation of the Mixed inhibitor
Conclusion
Thus, the type of inhibition of an enzymatic reaction from the given data is collected in the presence and the absence of an inhibitor is mixed inhibition.
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