BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Allostery is generally defined as the process of regulation of protein function due to the binding of an effector – a ligand or another protein – in a site on the protein surface referred to as an allosteric center [6].

Detailed explanation-2: -Allosteric regulation is the term used to describe any case in which a protein’s function at one site is affected by the binding of a regulatory molecule to a separate site. It may result in either inhibition or stimulation of an enzyme’s activity.

Detailed explanation-3: -An allosteric site does not bind substrate, but instead binds another molecule that affects the enzyme’s regulation. When a molecule binds an allosteric site, it alters the enzyme’s shape, or conformation, which then changes how the enzyme functions.

Detailed explanation-4: -An inhibitor may bind to an enzyme and block binding of the substrate, for example, by attaching to the active site. This is called competitive inhibition, because the inhibitor “competes” with the substrate for the enzyme.

Detailed explanation-5: -Allosterism describes the change in the affinity for binding of a ligand or substrate that is caused by the binding of another ligand away from the active site (allosteric = other site).