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- Allosteric_enzyme abstract "Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector, which results in an apparent change in binding affinity at a different ligand binding site. This "action at a distance" through binding of one ligand affecting the binding of another at a distinctly different site, is the essence of the allosteric concept. Allostery plays a crucial role in many fundamental biological processes, including but not limited to cell signaling and the regulation of metabolism. Allosteric enzymes need not be oligomers as previously thought, and in fact many systems have demonstrated allostery within single enzymes.Whereas enzymes without coupled domains/subunits display normal Michaelis-Menten kinetics, most allosteric enzymes have multiple coupled domains/subunits and show cooperative binding. Generally speaking, such cooperativity results in allosteric enzymes displaying a sigmoidal dependence on the concentration of their substrates in positively cooperative systems. This allows most allosteric enzymes to greatly vary catalytic output in response to small changes in effector concentration. Effector molecules, which may be the substrate itself (homotropic effectors) or some other small molecule (Allosteric regulation#Types of allosteric rheterotropic effector), may cause the enzyme to become more active or less active by redistributing the ensemble between the higher affinity and lower affinity states. The binding sites for heterotropic effectors, called allosteric sites, are usually separate from the active site yet thermodynamically coupled. Allosteric Database (ASD, http://mdl.shsmu.edu.cn/ASD) provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules, including allosteric enzymes and their modulators. Each enzyme is annotated with detailed description of allostery, biological process and related diseases, and each modulator with binding affinity, physicochemical properties and therapeutic area.".
- Allosteric_enzyme wikiPageExternalLink default.asp?s=&n=&i=&v=&o=&ns=0&uid=0&rau=0.
- Allosteric_enzyme wikiPageExternalLink ASD).
- Allosteric_enzyme wikiPageID "6182049".
- Allosteric_enzyme wikiPageRevisionID "606689690".
- Allosteric_enzyme hasPhotoCollection Allosteric_enzyme.
- Allosteric_enzyme subject Category:Enzymes.
- Allosteric_enzyme type Abstraction100002137.
- Allosteric_enzyme type Activator114723079.
- Allosteric_enzyme type Catalyst114723628.
- Allosteric_enzyme type Chemical114806838.
- Allosteric_enzyme type Compound114818238.
- Allosteric_enzyme type Enzyme114732946.
- Allosteric_enzyme type Enzymes.
- Allosteric_enzyme type Macromolecule114944888.
- Allosteric_enzyme type Material114580897.
- Allosteric_enzyme type Matter100020827.
- Allosteric_enzyme type Molecule114682133.
- Allosteric_enzyme type OrganicCompound114727670.
- Allosteric_enzyme type Part113809207.
- Allosteric_enzyme type PhysicalEntity100001930.
- Allosteric_enzyme type Protein114728724.
- Allosteric_enzyme type Relation100031921.
- Allosteric_enzyme type Substance100019613.
- Allosteric_enzyme type Thing100002452.
- Allosteric_enzyme type Unit109465459.
- Allosteric_enzyme comment "Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector, which results in an apparent change in binding affinity at a different ligand binding site. This "action at a distance" through binding of one ligand affecting the binding of another at a distinctly different site, is the essence of the allosteric concept.".
- Allosteric_enzyme label "Allosteric enzyme".
- Allosteric_enzyme label "Enzima alostérica".
- Allosteric_enzyme label "别构酶".
- Allosteric_enzyme sameAs Enzima_alostérica.
- Allosteric_enzyme sameAs Entzima_alosteriko.
- Allosteric_enzyme sameAs m.0fvj2d.
- Allosteric_enzyme sameAs Q3321436.
- Allosteric_enzyme sameAs Q3321436.
- Allosteric_enzyme sameAs Allosteric_enzyme.
- Allosteric_enzyme wasDerivedFrom Allosteric_enzyme?oldid=606689690.
- Allosteric_enzyme isPrimaryTopicOf Allosteric_enzyme.