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Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.
Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term allostery comes from the Greek allos (ἄλλος), "other," and stereos (στερεὀς), "solid (object)." This is in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site.
Allosteric Database (ASD) [1] provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules. Allostery is the most direct and efficient way for regulation of biological macromolecule function induced by the binding of a ligand at an allosteric site topographically ...
The site that an allosteric modulator binds to (i.e., an allosteric site) is not the same one to which an endogenous agonist of the receptor would bind (i.e., an orthosteric site). Modulators and agonists can both be called receptor ligands. [2] Allosteric modulators can be 1 of 3 types either: positive, negative or neutral.
Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ...
A regulatory enzyme is an enzyme in a biochemical pathway which, through its responses to the presence of certain other biomolecules, regulates the pathway activity. This is usually done for pathways whose products may be needed in different amounts at different times, such as hormone production.
Binding sites incur functional changes in a number of contexts, including enzyme catalysis, molecular pathway signaling, homeostatic regulation, and physiological function. Electric charge , steric shape and geometry of the site selectively allow for highly specific ligands to bind, activating a particular cascade of cellular interactions the ...
This is a diagram of allosteric regulation of an enzyme. When inhibitor binds to the allosteric site the shape of active site is altered, so substrate cannot fit into it. An allosteric site is a site on an enzyme, unrelated to its active site, which can bind an effector molecule. This interaction is another mechanism of enzyme regulation.