<Dd> 1 V = K m + (S) V max (S) = K m V max 1 (S) + 1 V max (\ displaystyle (1 \ over V) = ((K_ (m) + (S)) \ over V_ (\ max) (S)) = (K_ (m) \ over V_ (\ max)) (1 \ over (S)) + (1 \ over V_ (\ max))) </Dd> <P> where V is the reaction velocity (the reaction rate), K is the Michaelis--Menten constant, V is the maximum reaction velocity, and (S) is the substrate concentration . </P> <P> The Lineweaver--Burk plot was widely used to determine important terms in enzyme kinetics, such as K and V, before the wide availability of powerful computers and non-linear regression software . The y - intercept of such a graph is equivalent to the inverse of V; the x-intercept of the graph represents − 1 / K. It also gives a quick, visual impression of the different forms of enzyme inhibition . </P> <P> The double reciprocal plot distorts the error structure of the data, and it is therefore unreliable for the determination of enzyme kinetic parameters . Although it is still used for representation of kinetic data, non-linear regression or alternative linear forms of the Michaelis--Menten equation such as the Hanes - Woolf plot or Eadie--Hofstee plot are generally used for the calculation of parameters . </P>

From the lineweaver-burk plot which kinetic parameter can be determined from the y-intercept
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