allosteric

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Related to Allosteric regulation: feedback inhibition, Allosteric enzyme, covalent modification

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

(al'ō-ster'ik),
Pertaining to or characterized by allosterism.

allosteric

/al·lo·ster·ic/ (al″o-ster´ik) pertaining to allostery.

allosteric

(ăl′ə-stĕr′ĭk)
adj.
Of or relating to the binding of a molecule to an enzyme at a site other than the active site, resulting in modulation of the enzyme's activity as a result of a change in its shape.

al′lo·ster′i·cal·ly adv.
al·los′ter·y (ə-lŏs′tə-rē) n.

allosteric

Biochemistry
adjective
(1) Referring to allostery, see there.
(2) Referring to the alteration of a binding site on a protein, usually an enzyme, due to interaction with another molecule.
 
Molecular biology
adjective Referring to the stereospecific modification of a protein by an effector to influence other protein- or nucleic acid-binding site activity.

al·lo·ste·ric

(al'ō-ster'ik)
Pertaining to or characterized by allosterism.

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 ?
The results of the dynamic sensitivity analysis revealed that the metabolites in the methionine cycle behave stably as a result of perturbation to the enzymatic activity but have a possibility to oscillate in the absence of the allosteric regulation of CBS by AdoMet.