Allosteric regulation
Allosteric regulation (pronunciation: al-uh-ster-ik reg-yuh-ley-shuhn) is a process that directly impacts the activity and function of proteins and enzymes within a biological system.
Etymology
The term "allosteric" is derived from the Greek words "allos" meaning "other" and "stereos" meaning "solid". This refers to the effect that the binding of a molecule at one site on a protein can have on the protein's function at a different site.
Definition
Allosteric regulation is a mechanism of enzyme activity regulation in which a molecule that is not the enzyme's substrate binds to a location on the enzyme, causing a change in the enzyme's shape and affecting its ability to bind to the substrate. This location is known as the allosteric site.
Types of Allosteric Regulation
There are two main types of allosteric regulation: positive and negative.
- Positive Allosteric Regulation occurs when the binding of a molecule to the allosteric site increases the enzyme's activity.
- Negative Allosteric Regulation occurs when the binding of a molecule to the allosteric site decreases the enzyme's activity.
Related Terms
- Allosteric site: The location on an enzyme where a molecule that is not the enzyme's substrate can bind, causing a change in the enzyme's shape and affecting its ability to bind to the substrate.
- Allosteric inhibitor: A molecule that binds to an allosteric site and reduces the activity of an enzyme.
- Allosteric activator: A molecule that binds to an allosteric site and increases the activity of an enzyme.
- Cooperativity: A phenomenon in biology where the shape of one subunit of an enzyme consisting of several subunits is altered by the substrate or some other molecule so as to change the shape of neighboring subunits.
See Also
External links
- Medical encyclopedia article on Allosteric regulation
- Wikipedia's article - Allosteric regulation
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