Search results
Results from the WOW.Com Content Network
Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works. This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition.
An example of a neurotoxin are the glycoalkaloids, from the plant species in the family Solanaceae (includes potato, tomato and eggplant), that are acetylcholinesterase inhibitors. Inhibition of this enzyme causes an uncontrolled increase in the acetylcholine neurotransmitter, muscular paralysis and then death.
Competitive inhibitors are commonly used to make pharmaceuticals. [3] For example, methotrexate is a chemotherapy drug that acts as a competitive inhibitor. It is structurally similar to the coenzyme, folate, which binds to the enzyme dihydrofolate reductase. [3]
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 ...
Cells utilize product inhibition to regulate of metabolism as a form of negative feedback controlling metabolic pathways. [2] Product inhibition is also an important topic in biotechnology, as overcoming this effect can increase the yield of a product, such as an antibiotic. [3] Product inhibition can be competitive, non-competitive or ...
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 is distinguished from general mixed inhibition in that the inhibitor has an equal affinity for the enzyme and the enzyme-substrate complex. For example, in the enzyme-catalyzed reactions of glycolysis, accumulation phosphoenol is catalyzed by pyruvate kinase into pyruvate.
It acts as an inhibitor, binding a ligand and keeping it from binding to its regular receptor. Decoy receptors participate in common methods of signal inhibition and are also abundant in malignant tissues, making up a significant topic in cancer research. [1] Decoy receptors/ bind to ligands and inhibit signaling through actual receptors.