Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor.

[S] (mM)	vₒ (mM min⁻¹)	vₒ with I present (mM min⁻¹)
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

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.

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. ∝ 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 ∝ˈ. If there is an inhibitor, ∝ and ∝ˈ 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.

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.