How do negative allosteric ligands affect the Lineweaver-Burk plot?

Negative allosteric ligands decrease the affinity of an enzyme for its substrate, which results in an increase in the apparent Km (Michaelis constant) while the Vmax (maximum velocity) may remain unchanged or be affected depending on the specific nature of the allosteric interaction.

In the context of the Lineweaver-Burk plot, which is a double-reciprocal plot of 1/V versus 1/[S], an increase in Km due to negative allosteric modulation would manifest as a rightward shift of the plot. This shift occurs because as the value of Km increases, the slope of the line (which represents Km/Vmax) becomes steeper, leading to the appearance of the line being shifted to the right along the x-axis.

Thus, the correct interpretation of the effects of negative allosteric ligands is that they result in a shift of the Lineweaver-Burk plot to the right, reflecting the reduced substrate affinity.