allosteric site


Also found in: Dictionary, Thesaurus, Legal, Financial, Encyclopedia, Wikipedia.
Related to allosteric site: competitive inhibition

allosteric

 [al″o-ster´ik]
pertaining to an effect produced on the biological function of a protein by a compound not directly involved in that function (an allosteric effector) or to regulation of an enzyme involving cooperativity between multiple binding sites (allosteric sites).
allosteric site that subunit of an enzyme molecule which binds with a nonsubstrate molecule, inducing a change in form or shape that results in inactivation of the enzyme for its substrate.

al·lo·ste·ric site

postulated as the place on an enzyme, other than the active site, where a compound, which may be the ultimate product of the biosynthetic pathway involving the enzyme, may bind and influence the activity of the enzyme by changing the enzyme's conformation; the influence of CTP on aspartate carbamoyltransferase activity exemplifies the concept of an allosteric site on an allosteric protein.

al·lo·ste·ric site

(al'ō-ster'ik sīt)
Postulated as the place on an enzyme, other than the active site, where a compound, which may be the ultimate product of the biosynthetic pathway involving the enzyme, may bind and influence the activity of the enzyme by changing the enzyme's conformation.

allosteric site

a functional on/off switch for an enzyme situated away from its active site.

allosteric

pertaining to an effect on the biological function of a protein, produced by a compound not directly involved in that function (an allosteric effector) or to regulation of an enzyme involving cooperativity between multiple binding sites (allosteric sites).

allosteric enzymes
any enzymes containing an allosteric site, where effector molecules can bind to increase or decrease the rate of reaction, in addition to an active site for substrate binding. Allosteric enzymes exhibit sigmoidal rather than Michaelis-Menten kinetics.
allosteric site
that site on an enzyme molecule which binds with a nonsubstrate molecule, inducing a conformational change that results in an alteration of the affinity of the enzyme for its substrate.
References in periodicals archive ?
Locus' inflammation program has identified several lead series that demonstrate low nanomolar potency and high selectivity by targeting the allosteric site of p38 kinases.
In addition, the competition profiles indicate whether the compounds are binding to the same site on the protein as the competitor, or whether they are binding to a different, allosteric site.