he correct statement about allostery is:

Allosteric regulators are often products of other chemical reactions in the same biochemical

pathway.

Explanation

Let's break down each statement:

1. Allosteric regulators are often products of other chemical reactions in the same

biochemical pathway.

This statement is true. Allosteric regulators can indeed be products of other reactions in the same

pathway. This is a common mechanism of feedback regulation in biochemical pathways. When

the product of a pathway is abundant, it can bind to an enzyme earlier in the pathway and inhibit

its activity, preventing the production of more product.

2. Allosteric regulation is always used for negative regulation of enzyme activity.

This statement is false. Allosteric regulation can result in either inhibition (negative regulation)

or activation (positive regulation) of enzyme activity. The effect depends on whether the

allosteric regulator stabilizes the active or inactive form of the enzyme.

3. Binding of allosteric molecules usually locks an enzyme in its current conformation,

such that the enzyme cannot adopt a different conformation.

This statement is false. The binding of allosteric regulators can induce a conformational change

in the enzyme, shifting it between active and inactive states. It does not "lock" the enzyme in its

current conformation.

4. Enzymes are the only types of proteins that are subject to allosteric regulation.
This statement is false. While enzymes are a common target of allosteric regulation, they are not

the only proteins that can be allosterically regulated. Other proteins, such as transport proteins

and receptor proteins, can also be subject to allosteric regulation.