What is the Allosteric Inhibitor? Explain With an Example

By BYJU'S Exam Prep

Updated on: September 25th, 2023

Allosteric inhibitor is a molecule which combines with enzymes at allosteric site. ATP is an example of allosteric inhibitor.

A drug that interacts with an enzyme at an allosteric site is known as an allosteric inhibitor.
The allosteric site is located differently than the active site.
The inhibitor modifies the enzyme’s three-dimensional shape.
Allosteric inhibition includes non-competitive inhibition.

Examples of allosteric inhibitor:

ATP is a typical allosteric inhibitor (adenosine triphosphate).
The phosphofructokinase enzyme is responsible for glycolysis. ATP is created from the compound ADP (adenine diphosphate).
When ATP levels are too high, it functions as an allosteric inhibitor.
ATP and phosphofructokinase together cause ADP to be transformed more slowly. In this method, ATP stops unnecessary self-generation.

Table of content

ATP –

Adenosine triphosphate, also known as ATP, is referred to as the money of the cell.
It is an organic molecule made up of ribose, adenine, and phosphate groups. These molecules give the body’s many metabolic functions energy. As a result, it is referred to as Energy Currency of the Cell. The mitochondria are known as the powerhouse of the cell because they produce these ATP molecules.
German chemist Karl Lohmann made the discovery of the ATP molecule in 1929. The ATP molecule was initially created by Scottish biochemist Alexander Todd in the latter part of 1948.
All living species’ cells contain the energy-carrying molecules ATP. These organic molecules work by storing the chemical energy from the molecules of the meal that have been digested, which is then released for various cellular operations.

Summary:-

A chemical known as an allosteric inhibitor reacts with enzymes at their allosteric location. An illustration of an allosteric inhibitor is ATP.

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