Question

Which statement is FALSE about allosteric regulation?

Cellular response is faster with allosteric control than by controlling enzyme concentration in the cell.
The regulation usually is important to the conservation of energy and materials in cells.
Allosteric modulators bind non-covalently at sites other than the active site and induce conformational changes in the enzyme.
It is usually the mode of regulation for the last step in reaction pathways since this step produces the final product.

Answer 1

Answer:

It is usually the mode of regulation for the last step in reaction pathways since this step produces the final product.

Explanation:

Some enzyme are allosterically regulated in which an effector molecule regulate the activity of enzyme by binding to it other than the active site. That site is known as allosteric site. These effector molecules change the conformation, shape and functions of enzyme and may be either allosteric activators (enhance enzyme activity) or allosteric inhibitors (decrease protein activity).

Coopertivity is the process in which substrate itself act as allosteric activator and increase the activity of enzyme by binding to one active site.

Cellular response is faster with allosteric control than by controlling enzyme concentration in the cell because controlling the enzyme concentration would involve the Central Dogma process, which would take time.

Allosteric regulation is not specified to last step of reaction because it decrease or increase the speed of reaction. The last step depends on initial steps.

Answer 2

Allosteric regulation is the control of an enzyme that regulates its binding to an effector on a site other than the active site of an enzyme. This site other than the active site is known as regulatory or the allosteric site.

The false statement is:

Option D. It is generally the manner of regulation for the final step in reaction pathways since this stage yields the outcome.

The regulation can be explained as:

• The effector molecules alter the conformation and dimensions of the enzyme that modifies the role of enzymes.

• The allosteric molecules can either activate or inhibit reactions that is they can enhance or decrease enzyme activities.

• When the substrate acts as allosteric molecules itself then it is called cooperativity and it increases the activity of the enzyme.

• The use of allosteric molecules to upsurge the rate of reaction is more convenient than regulating enzymes as the controlling enzyme mechanism involves the processes of central dogma.

Therefore, the last step is not regulated by allosteric molecules.

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