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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 enzymes are enzymes that change their conformational ensemble upon binding of an effector (allosteric modulator) 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 ...
Glucose-6-phosphate isomerase (GPI), alternatively known as phosphoglucose isomerase/phosphoglucoisomerase (PGI) or phosphohexose isomerase (PHI), is an enzyme ( EC 5.3.1.9) that in humans is encoded by the GPI gene on chromosome 19. [4]
The inhibition of glycogen phosphorylase has been proposed as one method for treating type 2 diabetes. [10] Since glucose production in the liver has been shown to increase in type 2 diabetes patients, [11] inhibiting the release of glucose from the liver's glycogen's supplies appears to be a valid approach. The cloning of the human liver ...
CTP is also subject to various forms of allosteric regulation. GTP acts as an allosteric activator that strongly promotes the hydrolysis of glutamine, but is also inhibiting to glutamine-dependent CTP formation at high concentrations. [14] This acts to balance the relative amounts of purine and pyrimidine nucleotides. The reaction product CTP ...
Non-competitive inhibition models a system where the inhibitor and the substrate may both be bound to the enzyme at any given time. When both the substrate and the inhibitor are bound, the enzyme-substrate-inhibitor complex cannot form product and can only be converted back to the enzyme-substrate complex or the enzyme-inhibitor complex.
Inhibition of FBPase through proteolytic digestion decreases gluconeogenesis relative to glycolysis during cold periods, similar to hibernation. [18] Fructose 1,6-bisphosphate aldolase is another temperature dependent enzyme that plays an important role in the regulation of glycolysis and gluconeogenesis during hibernation. [14]
An allosteric transition of a protein between R and T states, stabilised by an Agonist, an Inhibitor and a Substrate. In biochemistry , the Monod–Wyman–Changeux model ( MWC model , also known as the symmetry model or concerted model ) describes allosteric transitions of proteins made up of identical subunits.