What does the slope of a Lineweaver Burk plot represent?

On the graph, the x-intercept can be used to determine the Michaelis constant, the y-intercept can be used to determine the maximal velocity and the slope represents the ratio of the Michaelis constant to the maximal velocity.

What is the Lineweaver Burk equation?

The Lineweaver-Burk equation is a linear equation, where 1/V is a linear function of 1/[S] instead of V being a rational function of [S]. The Lineweaver-Burk equation can be readily represented graphically to determine the values of Km and Vmax.

What are the advantages of the Lineweaver Burk plot?

For instance; Lineweaver-Burke plot, the most favoured plot by researchers, has two distinct advantages over the Michaelis-Menten plot, in that it gives a more accurate estimate of Vmax and more accurate information about inhibition. It increases the precision by linearizing the data.

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 is the significance of using the Lineweaver-Burk equation?

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 does the Michaelis Menten equation describe?

The Michaelis–Menten equation is mainly used to characterize the enzymatic rate at different substrate concentrations, but it is also widely applied to characterize the elimination of chemical (the first-order kinetics) compounds from the body.

Why is Michaelis important?

The Michaelis-Menten equation has been used to predict the rate of product formation in enzymatic reactions for more than a century. As substrate concentrations increase, a tipping point can be reached where an increase in the unbinding rate results in an increase, rather than a decrease, of the reaction rate.

What is the Michaelis Menten hypothesis equation formula?

The Michaelis-Menten equation arises from the general equation for an enzymatic reaction: E + S ↔ ES ↔ E + P, where E is the enzyme, S is the substrate, ES is the enzyme-substrate complex, and P is the product. The fraction [E][S]/[ES] has been coined Km, or the Michaelis constant.

Why is the Michaelis-Menten equation important?

What is the Michaelis-Menten kinetic scheme and how does this explain generally the observed kinetics?

What is the Michaelis-Menten kinetic scheme and how does this explain generally the observed kinetics? This scheme generally explains the observed kinetics since it shown the rate being proportional to the amount of E. S whose quantities are proportional to the amount of E and S.