Allosteric control: Difference between revisions

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Allosteric control or regulation, is when a molecule effects the action of an enzyme, by binding, but NOT to the active site, they bind to a specific allosteric site. On binding, they typically switch on/increase protein activity, or switch off/decrease protein activity. They cause these changes in levels of activity in the enzyme by causing a conformational change in the protein, leading to an alteration in the enzyme's active site, which therefore effects catalytic activity. They form part of a complex system of negative feedback and feedback loops.
Allosteric control or regulation, is when a [[Molecule|molecule]] effects the action of an [[enzyme|enzyme]], by binding, but NOT to the active site, they bind to a specific allosteric site. On binding, they typically switch on/increase [[protein|protein]] activity, or switch off/decrease protein activity. They cause these changes in levels of activity in the enzyme by causing a conformational change in the protein, leading to an alteration in the enzyme's active site, which therefore effects catalytic activity. They form part of a complex system of [[negative feedback|negative feedback]] and feedback loops <ref>http://www.biology.arizona.edu/biochemistry/problem_sets/energy_enzymes_catalysis/03t.html</ref>.<br>
 
=== References  ===
 
<references /><br>

Latest revision as of 04:39, 24 October 2014

Allosteric control or regulation, is when a molecule effects the action of an enzyme, by binding, but NOT to the active site, they bind to a specific allosteric site. On binding, they typically switch on/increase protein activity, or switch off/decrease protein activity. They cause these changes in levels of activity in the enzyme by causing a conformational change in the protein, leading to an alteration in the enzyme's active site, which therefore effects catalytic activity. They form part of a complex system of negative feedback and feedback loops [1].

References