allosteric

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Related to allosterically: gluconeogenesis

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 ?
Valerian extracts (VE) allosterically modulate GABAA receptors, an activity related to valerenic acid (Trawler et al.
The results listed in Table 1 demonstrate that binding properties of the ATP and peptide binding sites of protein kinase A were, indeed, allosterically coupled, and the effect of cooperativity was quantified by the interaction factor a.
The Company is engaged in the licensing of pepducin technology as research tools for drug development and has established a portfolio of first-in-class pepducin drug candidates, novel molecules that can selectively target G protein coupled receptors (GPCR) to allosterically modulate GPCR signaling.
The molecular mechanism of this action seems to be based on the ability of Hsp90 to allosterically activate/modulate eNOS (12).
However, the anti-inflammatory mefenamic acid, which is structurally similar to loreclezole, did inhibit valerenic acid binding, which suggests that valerenic acid may bind to an as yet unrecognized site that is allosterically linked to anesthetics and mefenamic acid.
The mechanism by which ion channels carry out these presumably allosterically modulated conformational changes can be perturbed by the brevetoxins.
Lassos can be allosterically regulated, enabling them to respond to the environment and potentially making them cell-specific.
Anchor Therapeutics is developing first-in-class pepducin drug candidates, novel molecules that can selectively target G protein coupled receptors (GPCRs) to allosterically modulate GPCR signaling.
GDH is normally activated by leucine and ADP and allosterically inhibited by GTP and ATP.
It is a reversible competitive AChE inhibitor that also allosterically modulates nicotinic receptors (this effect is probably independent of its cholinesterase inhibition).
The highly charged S4 helix in each domain is thought to respond allosterically to changes in membrane potential, a "voltage sensor.