What is a Lineweaver-Burk plot and why is it useful?
The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, 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 Vmax; the x-intercept of the graph represents −1/Km.
What is a Lineweaver-Burk plot competitive inhibition?
Lineweaver Burk Plots and Enzyme Inhibition In terms of competitive inhibitors, recall that they compete directly with the substrate to bind to the active site of the enzyme. In turn, they will decrease the affinity of the enzyme for the substrate, which will increase the KM.
What does the Michaelis Menten equation tell us?
The Michaelis–Menten equation (Eqn (4)) is the rate equation for a one-substrate enzyme-catalyzed reaction. This equation relates the initial reaction rate (v0), the maximum reaction rate (Vmax), and the initial substrate concentration [S] through the Michaelis constant KM—a measure of the substrate-binding affinity.
What does the Michaelis-Menten plot show?
In a classic Michaelis-Menten graph, the y-axis represents reaction rate and the x-axis represents substrate concentration. At low substrate concentrations, the reaction rate increases sharply.
Why is Michaelis constant important?
Significance of Michaelis-Menten Constant: (i) By knowing the Km value of a particular enzyme-substrate system, one can predict whether the cell needs more enzymes or more substrate to speed up the enzymatic reaction.
Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?
Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve? because any deviations would not be noticed in a curve but would be immediately noticed in a straight line.