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 ?
Some parasite GDHs, like the mammalian enzymes, are allosterically modified by nucleotides [30].
The non-nucleoside polymerase inhibitors are drugs which bind allosterically on the enzyme surface near to its active site to disturb its structure and function.
This enzymatic reaction is allosterically activated by the so-called ADP-ribosylation factors (ARFs), a family of essential and ubiquitous G proteins.
Recently it was shown that the binding effectiveness of ATP analogue [beta], [gamma]-imidoadenosine 5'-triphosphate (AMPPNP) and peptide substrate LRRASLG (kemptide) with protein kinase A is effectively controlled allosterically [13].
A] receptors) to enhance receptor function allosterically by producing a conformation, or shape, change in the receptor (Mitchell et al.
Ligand binding to the peripheral site can block access of substrates or allosterically alter the catalytic efficiency of AChE, but more importantly for our considerations, it interferes with its nonenzymatic adhesion functions that are required for axonogenesis and other developmental events (Bourne et al.
It is possible that changes in the concentration of glucose-6-phosphate during germination could increase the rate of glycogen synthesis by allosterically activating the glucose-6-phosphate-dependent glycogen synthase.
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 peptide binds complement C5 with sub-nanomolar affinity and allosterically inhibits its cleavage into C5a and C5b upon activation of the classical, alternative or lectin pathways.
Valerian extracts allosterically modulate GABAA receptors, an action related to valerenic acid, which is one of the active compounds determined from pharmacological studies.