Virtual Enzyme Kinetics & Lineweaver Burk Plot

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HWC

• The double-reciprocal (also known as the Lineweaver-Burk) plot is created by plotting the inverse initial velocity (1/V0) as a function of the inverse of the substrate concentration (1/[S]). • This plot is a useful way to determined different inhibitors such as competitive, uncompetitive, and noncompetitive. • Chemical kinetics and enzyme kinetics are related, but enzyme kinetics necessitates different treatment because of the substrate's complex with enzyme catalyst. • Michaelis Menten kinetics describes enzyme-catalyzed reactions. • Vmax is the maximum velocity at saturating [S]. • KM determines shape of Michaelis Menten hyperbolic curve. • Data from kinetic experiments can be plotted as a Michaelis-Menten curve or as a line in a double-reciprocal plot. The resulting graphs can be interpreted to obtain Vmax and Km.

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