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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.
More recently, the E. coli enzyme aspartate carbamoyltransferase (ATCase) has become another good example of allosteric regulation. The kinetic properties of allosteric enzymes are often explained in terms of a conformational change between a low-activity, low-affinity "tense" or T state and a high-activity, high-affinity "relaxed" or R state.
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.
[1] [2] Non-competitive inhibition is sometimes thought of as a special case of mixed inhibition. In mixed inhibition, the inhibitor binds to an allosteric site, i.e. a site different from the active site where the substrate binds. However, not all inhibitors that bind at allosteric sites are mixed inhibitors. [1] Mixed inhibition may result in ...
They are the opposite of enzyme inhibitors. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. In some cases, when a substrate binds to one catalytic subunit of an enzyme, this can trigger an increase in the substrate affinity as well as catalytic activity in the enzyme's other subunits, and ...
Alanine is a non-competitive inhibitor, therefore it binds away from the active site to the substrate in order for it to still be the final product. [6] Another example of non-competitive inhibition is given by glucose-6-phosphate inhibiting hexokinase in the brain. Carbons 2 and 4 on glucose-6-phosphate contain hydroxyl groups that attach ...
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 ...