Allosteric inhibition
Allosteric inhibition (pronunciation: al-uh-ster-ik in-hi-bi-shun) is a process that directly impacts the biochemical activity within an organism. It is a form of regulation where the function of a protein is modified due to the binding of an effector molecule at a site other than the protein's active site.
Etymology
The term "allosteric inhibition" is derived from the Greek words "allos" meaning "other" and "stereos" meaning "solid". This refers to the change in the solid state of the protein when an effector molecule binds to it at a site other than the active site.
Process
In allosteric inhibition, an allosteric inhibitor binds to an allosteric site, which is different from the active site of the protein. This binding causes a conformational change in the protein's structure, which in turn alters the shape of the active site. As a result, the substrate cannot bind to the active site, inhibiting the protein's function.
Related Terms
- Allosteric site: The site on an enzyme where the allosteric inhibitor binds.
- Allosteric inhibitor: The molecule that binds to the allosteric site and inhibits the function of the enzyme.
- Active site: The region of an enzyme where substrate molecules bind and undergo a chemical reaction.
- Substrate: The molecule upon which an enzyme acts.
See Also
External links
- Medical encyclopedia article on Allosteric inhibition
- Wikipedia's article - Allosteric inhibition
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