Alternative models developed by C.S. Hanes or B.H.J. Hofstee and G.S. Eadie are preferred to this error-prone one. The Briggs-Haldane assumption is used in the formulation of this model. Non-competitive inhibitors decrease maximum reaction velocity but do not affect an eponymous constant, so that the slope rises, but the x-intercept is unchanged. Competitive inhibitors bind the enzyme, increasing the Michaelis constant, so that the slope increases, but the y-intercept is unchanged. Representing the reciprocal of reaction rate plotted against the reciprocal of substrate concentration, name, for 10 points, this doubly eponymous biochemical plot from enzyme kinetics that is used to graphically 
Alternative models developed by C.S. Hanes or B.H.J. Hofstee and G.S. Eadie are preferred to this error-prone one. The Briggs-Haldane assumption is used in the formulation of this model. Non-competitive inhibitors decrease maximum reaction velocity but do not affect an eponymous constant, so that the slope rises, but the x-intercept is unchanged. Competitive inhibitors bind the enzyme, increasing the Michaelis constant, so that the slope increases, but the y-intercept is unchanged. Representing the reciprocal of reaction rate plotted against the reciprocal of substrate concentration, name, for 10 points, this doubly eponymous biochemical plot from enzyme kinetics that is used to graphically represent the Michaelis-Menten equation.
Alternative models developed by C.S. Hanes or B.H.J. Hofstee and G.S. Eadie are preferred to this error-prone one.
{Lineweaver}-{Burk} plot [prompt on “{double}-{reciprocal}” {plot}]