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Therefore, because of sulfa drugs' competitive inhibition, they are excellent antibacterial agents. An example of competitive inhibition was demonstrated experimentally for the enzyme succinic dehydrogenase, which catalyzes the oxidation of succinate to fumarate in the Krebs cycle. Malonate is a competitive inhibitor of succinic dehydrogenase ...
An enzyme inhibitor is characterised by its dissociation constant K i, the concentration at which the inhibitor half occupies the enzyme. In non-competitive inhibition the inhibitor can also bind to the enzyme-substrate complex, and the presence of bound substrate can change the affinity of the inhibitor for the enzyme, resulting in a second ...
Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e. initiates or enhances) the expression of an enzyme. 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.
Substrate analogs (substrate state analogues), are chemical compounds with a chemical structure that resemble the substrate molecule in an enzyme-catalyzed chemical reaction. Substrate analogs can act as competitive inhibitors of an enzymatic reaction. An example is phosphoramidate to the Tetrahymena group I ribozyme. [1]
A competitive inhibitor and substrate cannot bind to the enzyme at the same time. [74] Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, the drug methotrexate is a competitive inhibitor of the enzyme dihydrofolate reductase, which catalyzes the reduction of dihydrofolate to tetrahydrofolate. [75]
Most inhibitors of CYP2C9 are competitive inhibitors. Noncompetitive inhibitors of CYP2C9 include nifedipine, [39] [40] phenethyl isothiocyanate, [41] medroxyprogesterone acetate [42] and 6-hydroxyflavone. It was indicated that the noncompetitive binding site of 6-hydroxyflavone is the reported allosteric binding site of the CYP2C9 enzyme. [43]
As glucokinase is a monomeric enzyme with only a single binding site [16] for glucose the cooperativity cannot be explained in terms of classical models of equilibrium cooperativity, but requires a kinetic explanation, such as a slow-transition model [17] or a "memonical" model that invokes enzyme memory. [18]
In competitive inhibition, the inhibitor binds to the active site, thus preventing enzyme-substrate interaction. In non-competitive inhibition, the inhibitor binds to an allosteric site, which alters the active site and makes it inaccessible to the substrate. Examples of protease inhibitors include: Serpins; Stefins; IAPs
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