allosteric


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Related to allosteric: allosteric site

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 ?
While many of the mutations block Gleevec from plugging into the kinase domain, others appear to interfere with the allosteric regulation.
We showed that p,p'-DDT potentiates the maximum FSH-stimulated cAMP production by the FSHR and thus acts as a positive allosteric modulator.
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.
Since some of these enzymes fuction as allosteric modifies in intra-cellular reactions, the fluctuations inevitably affect these reactions [13,14].
We believe this work represents a breakthrough in designing synthetic allosteric agonists for chemokine GPCRs," said Thomas Sakmar, M.
Depending on the [alpha] value, the binding of one substrate can favour ([alpha] < 1) or hinder ([alpha] > 1) the binding of the second substrate, leading to a positive or negative effect of allosteric cooperativity.
Gilliland, Positive and Negative Cooperativitics at Subsequent Steps of Oxygenation Regulate the Allosteric Behavior of Sebacyl-Hemoglobin, Biochemistry 35 (11), 3418-3425 (1996).
Clearly, the expression of proteins with the correct conformational and allosteric properties is essential for cells to perform their specific function(s).
Company successfully discovered and optimized the first small molecule allosteric inhibitors of ACC achieving excellent potency, selectivity and drug-like properties within 12 months -
ADX71441 is a potent, selective positive allosteric modulator (PAM) that potentiates GABA responses at the GABAB receptor.
The current project aims at deciphering the molecular and pharmacological determinants of positive allosteric modulators of neuronal nicotinic receptors.
Targeting scientists looking to understand the practice of fragment-based drug discovery (FBDD), Howard and Abell provide experts from the areas of epigenetics, G protein-coupled receptors (GPCRs), protein-protein interactions, antibacterials and identification of novel allosteric binding pockets, and discuss lessons learned based on experience and key examples from the literature.