Answer:
In allosteric inhibition, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate.
Explanation:
Allosteric regulation of an enzyme can be positive or negative, but it always involves effector molecules that bind to non-active site of the enzyme and change its conformation. That site of binding is called allosteric or regulatory site. If the enzyme activity is enhanced effector molecule is called allosteric activator but if the activity is decreased effector molecules are allosteric inhibitors.
1. The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation).
2. Carbon has four valence electrons, so it can achieve a full outer energy level by forming four covalent bonds.
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