Question

Regarding the Lineweaver–Burk plot data, could you provide the sets of data or specifics on why each set might not be ideal for determining K_m​ for an enzyme-catalyzed reaction following Michaelis–Menten kinetics?

Answer 1

A Lineweaver–Burk plot may not be ideal for determining Km if the enzyme has an allosteric site, if the reaction involves multiple substrates, or if the enzyme is regulatory. These limitations can be overcome using a Lineweaver–Burk plot.

Step-by-step explanation:

A Lineweaver–Burk plot is a graphical representation used to analyze enzyme kinetics. However, there are certain sets of data that may not be ideal for determining Km for an enzyme-catalyzed reaction following Michaelis–Menten kinetics.

1. If the enzyme has both an active site and an allosteric site, the Lineweaver–Burk plot may not accurately determine Km because it only applies to enzymes with active sites.
2. If the enzyme-catalyzed reaction involves multiple substrates (multisubstrate reactions), the Lineweaver–Burk plot may not be suitable for determining Km because it is specifically designed for monosubstrate reactions.
3. The Lineweaver–Burk plot is more relevant for non-regulatory enzymes and may not provide accurate results for regulatory enzymes.

These limitations can be overcome by using a Lineweaver–Burk plot, which establishes a relationship between the reciprocals of substrate concentration and velocity.