(redirected from allosterically)
Also found in: Medical.
Related to allosterically: gluconeogenesis


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.


(Biochemistry) biochem of, relating to, or designating a function of an enzyme in which the structure and activity of the enzyme are modified by the binding of a metabolic molecule


(ˌæl əˈstɛr ɪk, -ˈstɪər-)

of or pertaining to a change in the activity of an enzyme at a site other than the binding site of the substrate.
al`lo•ster′i•cal•ly, adv.
References in periodicals archive ?
The peptide binds complement component 5 with sub-nanomolar affinity and allosterically inhibits its cleavage into C5a and C5b upon activation of the classical, alternative, or lectin pathways.
In contrast, PK2 is much less active but is allosterically activated by the upstream glycolytic metabolite fructose 1, 6-bisphosphate (FBP).
Additionally, vanillin can allosterically modulate the GABAergic neurotransmission by enhancing the binding of the endogenous receptor agonist (Ha et al.
According to the company, CpAMs are direct-acting antivirals that allosterically modulate core protein.
Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription.
Because the distance between the ATP-binding site and the actin-binding site is 4 nm, the effect of ATP binding is transferred allosterically to the actin-binding site.
Ethanol allosterically potentiates the action of GABA, or any other activator of this receptor as benzodiazepines or barbiturates, stimulating the flow of chloride induced by these [GABA.
Taxol allosterically alters the dynamics of the tubulin dimer and increases the flexibility of microtubules.
3]H] muscimol binding sites three-fold in rat forebrain membranes in vitro using a filtration assay, by allosterically increasing the affinities of low-affinity sites.
Pre-clinical and clinical data have illustrated that kinase inhibitors can allosterically activate or inhibit signaling, revealed mechanisms of resistance to targeted inhibitors, and importantly, demonstrated that differential binding modes can lead to vastly different functional effects.
27-29) One mechanism of resistance is mutation in the ALK gatekeeper region (L1196M), in a similar way to that seen with EGFR resistance mutations, possibly by interfering allosterically with the binding of tyrosine kinase inhibitors.