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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.
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.
Malonate is a competitive inhibitor of succinic dehydrogenase. The binding of succinic dehydrogenase to the substrate, succinate, is competitively inhibited. This happens because malonate's chemistry is similar to succinate. Malonate's ability to inhibit binding of the enzyme and substrate is based on the ratio of malonate to succinate.
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.
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 ...
Another example of allelopathy is seen in Leucaena leucocephala, known as the miracle tree. This plant contains toxic amino acids that inhibit other plants’ growth but not its own species growth. Different crops react differently to these allelochemicals, so wheat yield decreases, while rice increases in the presence of L. leucocephala .
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.
Stereoisomers of Soman, a G-series nerve agent and suicide inhibitor of acetylcholinesterase.Note the non-carbon chiral center.. In biochemistry, suicide inhibition, also known as suicide inactivation or mechanism-based inhibition, is an irreversible form of enzyme inhibition that occurs when an enzyme binds a substrate analog and forms an irreversible complex with it through a covalent bond ...