Allosteric activator
Allosteric Activator
Allosteric activator (pronunciation: al-uh-ster-ik ak-tuh-vey-ter) is a type of enzyme regulator that binds to an enzyme at a site other than the active site. This binding changes the conformation of the enzyme, enhancing its activity and increasing the rate of reaction.
Etymology
The term "allosteric activator" is derived from the Greek words "allos" meaning "other" and "stereos" meaning "solid". This refers to the fact that these activators bind to a different site on the enzyme, not the active site.
Function
Allosteric activators function by binding to a site on the enzyme that is distinct from the active site. This binding induces a conformational change in the enzyme, which in turn increases the enzyme's affinity for its substrate at the active site. This process is known as allosteric regulation, a key mechanism in cellular metabolism and homeostasis.
Related Terms
- Allosteric site: The site on an enzyme where the allosteric activator binds.
- Allosteric inhibition: A process that decreases enzyme activity through the binding of an allosteric inhibitor.
- Cooperativity: A phenomenon in multi-subunit enzymes where binding of a substrate to one active site affects the activity at other active sites.
- Enzyme kinetics: The study of the rates at which enzymes catalyze reactions.
See Also
External links
- Medical encyclopedia article on Allosteric activator
- Wikipedia's article - Allosteric activator
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