How Does Non-Competitive Inhibition Affect Enzyme Kinetics?
In enzyme kinetics, non-competitive inhibition affects both the maximum reaction rate (Vmax) and the enzyme's efficiency. The inhibitor binds to an allosteric site, which is distinct from the active site. This binding does not prevent the substrate from binding to the enzyme but inhibits the enzyme's catalytic activity. Consequently, Vmax decreases because the total number of active enzymes is reduced. However, the affinity of the enzyme for the substrate (Km) remains unchanged because the substrate can still bind to the enzyme.
