<P> The Lineweaver--Burk plot or double reciprocal plot is a common way of illustrating kinetic data . This is produced by taking the reciprocal of both sides of the Michaelis--Menten equation . As shown on the right, this is a linear form of the Michaelis--Menten equation and produces a straight line with the equation y = mx + c with a y - intercept equivalent to 1 / V and an x-intercept of the graph representing − 1 / K . </P> <Dl> <Dd> 1 v = K M V max (S) + 1 V max (\ displaystyle (\ frac (1) (v)) = (\ frac (K_ (M)) (V_ (\ max) ((\ mbox (S))))) + (\ frac (1) (V_ (\ max)))) </Dd> </Dl> <Dd> 1 v = K M V max (S) + 1 V max (\ displaystyle (\ frac (1) (v)) = (\ frac (K_ (M)) (V_ (\ max) ((\ mbox (S))))) + (\ frac (1) (V_ (\ max)))) </Dd> <P> Naturally, no experimental values can be taken at negative 1 / (S); the lower limiting value 1 / (S) = 0 (the y - intercept) corresponds to an infinite substrate concentration, where 1 / v = 1 / V as shown at the right; thus, the x-intercept is an extrapolation of the experimental data taken at positive concentrations . More generally, the Lineweaver--Burk plot skews the importance of measurements taken at low substrate concentrations and, thus, can yield inaccurate estimates of V and K. A more accurate linear plotting method is the Eadie - Hofstee plot . In this case, v is plotted against v / (S). In the third common linear representation, the Hanes - Woolf plot, (S) / v is plotted against (S). In general, data normalisation can help diminish the amount of experimental work and can increase the reliability of the output, and is suitable for both graphical and numerical analysis . </P>

What is an important characteristic of an enzyme