Which type of inhibition shifts the Lineweaver-Burk plot to the right?

In the context of enzyme kinetics, competitive inhibition is characterized by the inhibitor binding to the active site of the enzyme, competing directly with the substrate. This type of inhibition increases the apparent Km (Michaelis constant) because a higher concentration of substrate is required to reach half of the maximum reaction rate when the inhibitor is present.

On a Lineweaver-Burk plot, which is a double reciprocal plot of 1/v against 1/[S], competitive inhibition is represented by adjusting the x-intercept, shifting it to the right. This shift signifies the increased Km value while the Vmax remains unchanged. As a result, more substrate is needed to achieve the same enzyme activity in the presence of the competitive inhibitor.

In summary, competitive inhibition shifts the Lineweaver-Burk plot to the right due to the increased apparent Km resulting from the competition between the substrate and the inhibitor for the enzyme's active site.