پاورپوینت گلیکولیز
نوع فایل: پاورپوینت
قابل ویرایش 64 اسلاید
Allosteric enzymes are enzymes that change their conformation upon binding of an effector. An allosteric enzyme is an oligomer whose biological activity is affected by altering the conformation(s) of its quaternary structure. Allosteric enzymes tend to have several subunits. These subunits are referred to as protomers. In a given conformational state, these enzymes can bind substrate (S), inhibitor (l), and activator (A).
Whereas enzymes with single active sites display normal Michaelis-Menten kinetics, allosteric enzymes have multiple active sites and show cooperative binding. As a result, allosteric enzymes display a sigmoidal dependence on the concentration of their substrates, allowing them 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 (heterotropic effector), may cause the enzyme to become more active or less active. The binding sites for heterotropic effectors, called allosteric (Regulatory) sites, are separate from the active site
محصول نهایی یک مسیر بیوشیمیایی نیز می تواند در صورت افزایش غلظت آن به بالاتر از یک حد مشخص، موجب مهار آنزیم آلوستریک (آنزیم کلیدی در مسیر مورد نظر) گردد که به آن فیدبک منفی می گویند.

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