Which of the following describes the impact of mixed inhibition?

In mixed inhibition, an inhibitor can bind to both the enzyme and the enzyme-substrate complex, leading to changes in both the maximum reaction velocity (Vmax) and the apparent affinity of the enzyme for its substrate, represented by the Michaelis constant (Km). The presence of the inhibitor alters the reaction rates in a way that the lineweaver-burk plot, which portrays the relationship between the inverse of reaction velocity (1/V) and the inverse of substrate concentration (1/[S]), will show both x and y-intercepts being affected. This interaction results in a specific pivot point where the inhibition modifies the slope of the line without retaining its original position—the intercept changes depending on the concentration of the inhibitor.

This understanding of mixed inhibition is crucial since it demonstrates how different inhibitors can affect enzyme kinetics differently and highlights the intricate balance of enzyme-substrate interactions that can be manipulated in various biochemical pathways. The fact that both Km and Vmax are altered represents a signature feature of mixed inhibition, distinguishing it from other types of reversible inhibition.