Resultado de búsqueda
Malonic acid is the classic example of a competitive inhibitor of the enzyme succinate dehydrogenase (complex II), in the respiratory electron transport chain. It binds to the active site of the enzyme without reacting, competing with the usual substrate succinate but lacking the −CH 2 CH 2 − group required for dehydrogenation.
An example of competitive inhibition could be malonic acid which competes with succinate for active sites of succinic dehydrogenase, an important enzyme in the Krebs cycle. Another Example: Ethanol is metabolized in the body by oxidation to acetaldehyde, which is in turn further oxidized to acetic acid by aldehyde oxidase enzymes.
Malonate, a competitive inhibitor of succinate dehydrogenase of the TCA cycle, is a potent inhibitor of mitochondrial respiration. A major role for ACSF3 is to provide a metabolic pathway for the clearance of malonate by the generation of malonyl-CoA, which can then be decarboxylated to acetyl-CoA by malonyl-CoA decarboxylase.
Malonate acts as a competitive inhibitor of the enzyme succinate dehydrogenase, a key molecule in the tricarboxylic acid (TCA) cycle and electron transport chain (Kim, 2002).
Malonic acid is the archetypal instance of a competitive inhibitor: it functions in the respiratory electron transport chain against succinate dehydrogenase. Malonic acid is correlated with deficiency of malonyl-CoA decarboxylase, an inborn metabolism mistake.
A competitive inhibitor is any compound that bears a structural resemblance to a particular substrate and thus competes with that substrate for binding at the active site of an enzyme. The inhibitor is not acted on by the enzyme but does prevent the substrate from approaching the active site.
A well-known example is that of succinate dehydrogenase inhibition by malonate (ionized form of malonic acid). Succinate dehydrogenase catalyzes the oxidation of succinate, which loses two hydrogens to become fumarate.
