How do you use Lineweaver-Burk plots to analyze enzyme kinetics?

The Lineweaver-Burk plot (double reciprocal plot) linearizes the Michaelis-Menten equation: 1/v = (Km/Vmax)(1/[S]) + 1/Vmax. The y-intercept gives 1/Vmax, x-intercept gives -1/Km, and slope is Km/Vmax. This linear form enables graphical determination of kinetic parameters and identification of inhibition types. Competitive inhibitors increase slope without changing y-intercept (lines intersect on y-axis); non-competitive inhibitors increase y-intercept without changing x-intercept (lines intersect on x-axis); uncompetitive inhibitors increase both intercepts equally (parallel lines). Modern analysis uses nonlinear regression fitting directly to Michaelis-Menten equation for more accurate parameter estimation.