By using this site, you agree to the Terms of Use and Privacy Policy. For this exercise we need to set up columns for the various parameters in the Michaelis-Menten equation. Journal of Chromatography B. It also gives a quick, visual impression of the different forms of enzyme inhibition. The Lineweaver—Burk plot is classically used in older texts, but is prone to error, as the y -axis takes the reciprocal of the rate of reaction — in turn increasing any small errors in measurement. How do these values compare to each other and to the “real” values. Uncompetitive inhibition causes different intercepts on both the y – and x -axes. Plots graphics Enzyme kinetics.

For this exercise we need to set up columns for the various parameters in the Michaelis-Menten equation. How do these values compare to each other and to the “real” values. In other projects Wikimedia Commons. Next fill the substrate column with concentrations from 0 – 5 Go to Edit – Fill – Series , when the dialog box comes up click on the radio button for columns under Series in , then set the step value to 0. The Lineweaver—Burk plot was widely used to determine important terms in enzyme kinetics, such as K m and V max , before the wide availability of powerful computers and non-linear regression software. What are its problems? The Lineweaver—Burk plot is classically used in older texts, but is prone to error, as the y -axis takes the reciprocal of the rate of reaction — in turn increasing any small errors in measurement.

What are its problems? Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator.

This page was last edited on 16 Januaryat When used for determining the type of enzyme inhibition, the Lineweaver—Burk plot can distinguish competitivenon-competitive and uncompetitive inhibitors. Plots graphics Enzyme kinetics.

## Lineweaver–Burk plot

Set up your spread sheet as in the figure:. How do these values compare to each other and to the “real” values. Although it is still used for representation of kinetic data, [2] 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. Then change the value of Pllt m to 0.

In this exercise we will use a spreadsheet model to generate some plots of enzyme kinetic behavior. Journal of the American Chemical Society. From Wikipedia, the free excl.

The plot provides a useful graphical method for analysis of the Michaelis—Menten equation, as its difficult to determine precisely the Vmax of an enzyme catalysed reaction:.

### Chem M M Kinetics

Retrieved from ” https: Uncompetitive inhibition causes different intercepts on both the y – and x -axes. Next fill the substrate column with concentrations from 0 – 5 Go to Edit – Fill – Serieswhen the dialog box comes up click on the radio button for columns under Series inthen set the step value to 0. In biochemistrythe Lineweaver—Burk plot or double reciprocal plot is a graphical representation of the Lineweaver—Burk equation of enzyme kineticsdescribed by Hans Lineweaver and Dean Burk in Ignoring the known values for Km and Vmax, find them graphically from your plots.

Analogously to our titration exercise, we will use the M-M equation as our model for the enzyme reaction system. Now go back and add a line to the plot by going under ChartAdd Trendline.

The double reciprocal plot distorts the error structure of the data, and it is therefore unreliable for the determination of enzyme kinetic parameters. Competitive inhibitors have the same y -intercept as uninhibited enzyme since V max is unaffected by competitive inhibitors the inverse of V max also doesn’t change but there are different slopes and x -intercepts between the two data sets.

Journal of Biological Chemistry. Views Read Edit View history. For this exercise we need to set libeweaver columns for the various parameters in the Michaelis-Menten equation.

### Lineweaver–Burk plot – Wikipedia

Next plot your results. The same kinds of techniques we used before for the titration curves will be used.

Duplicate and copy your spread sheet columns capture the columns with the mouse, then click on a cell, say F, and hit enter:. How accurate and effective do you think this plot is for finding values from real data? By using this xecel, you agree to the Terms of Use and Linfweaver Policy. Go to Insert – Chart The Lineweaver—Burk plot was widely used to determine important terms in enzyme kinetics, such as K m and V maxbefore the wide availability of powerful computers and non-linear regression software.

In the dialog boxes choose linear, then double-click on the line and under options choose display equation and r-squared The Kineweaver plot is classically used in older texts, but is prone to error, as the y -axis takes the reciprocal of the rate of reaction — in turn increasing any small errors in measurement.

Make a new chart of this data, labeling appropriately etc. In other projects Wikimedia Commons. It also gives a quick, visual impression of the different forms of enzyme inhibition. EC number Enzyme superfamily Enzyme family List of enzymes. Journal of Chromatography B. Linewevaer inhibition produces plots with the same x -intercept as uninhibited enzyme K m is unaffected but different slopes and y -intercepts.