Question

Which of the following statements is the correct definition of an allosteric protein

a) The binding of a ligand to one site affects the properties at another site
b) The binding of a modulator is affected by ligand binding
c) The binding of a ligand is affect by the binding of oxygen
d) The binding of a ligand is not affected by the binding of oxygen

Answer 1

An allosteric inhibitor is a molecule that binds to an enzyme at a site other than the active site, causing a conformational change that decreases the enzyme's affinity for the substrate and inhibits its activity.

Step-by-step explanation:

In the context of enzyme regulation, an allosteric inhibitor binds to an enzyme at a site other than the active site, known as the allosteric site. This leads to a conformational change in the enzyme that decreases its affinity for the substrate. In other words, allosteric inhibition occurs when a regulatory molecule binds to the allosteric site of an enzyme, causing a conformational change to the active site. This change ultimately prevents substrate binding, thus reducing or preventing the enzyme's catalytic activity. Conversely, allosteric activators bind to regions on the enzyme away from the active site and induce a change that increases the enzyme's affinity for the substrate.