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Also acid ionization constant or acidity constant. A quantitative measure of the strength of an acid in solution expressed as an equilibrium constant for a chemical dissociation reaction in the context of acid-base reactions. It is often given as its base-10 cologarithm, p K a. acid–base extraction A chemical reaction in which chemical species are separated from other acids and bases. acid ...
An inhibitor can reduce the effectiveness of a catalyst in a catalysed reaction (either a non-biological catalyst or an enzyme).E.g., if a compound is so similar to (one of) the reactants that it can bind to the active site of a catalyst but does not undergo a catalytic reaction then that catalyst molecule cannot perform its job because the active site is occupied.
A competitive inhibitor could bind to an allosteric site of the free enzyme and prevent substrate binding, as long as it does not bind to the allosteric site when the substrate is bound. For example, strychnine acts as an allosteric inhibitor of the glycine receptor in the mammalian spinal cord and brain stem. Glycine is a major post-synaptic ...
Index inducer or just inducer predictably induce metabolism via a given pathway and are commonly used in prospective clinical drug-drug interaction studies. [2]Strong, moderate, and weak inducers are drugs that decreases the AUC of sensitive index substrates of a given metabolic pathway by ≥80%, ≥50% to <80%, and ≥20% to <50%, respectively.
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 ...
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.
The binding of an inhibitor and its effect on the enzymatic activity are two distinctly different things, another problem the traditional equations fail to acknowledge. In noncompetitive inhibition the binding of the inhibitor results in 100% inhibition of the enzyme only, and fails to consider the possibility of anything in between. [50]
The results of this study suggest that the mere presence of another person in a social situation can inhibit an individual; however, although the individual in charge of completing the experimental task was socially inhibited by the presence of another person in the laboratory, there were no significant links between their social inhibition ...