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  2. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Reversible inhibition can be described quantitatively in terms of the inhibitor's binding to the enzyme and to the enzyme-substrate complex, and its effects on the kinetic constants of the enzyme. [ 24 ] : 6 In the classic Michaelis-Menten scheme (shown in the "inhibition mechanism schematic" diagram), an enzyme (E) binds to its substrate (S ...

  3. Enzyme induction and inhibition - Wikipedia

    en.wikipedia.org/wiki/Enzyme_induction_and...

    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.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes can be either activated or inhibited by other molecules. For example, the end product(s) of a metabolic pathway are often inhibitors for one of the first enzymes of the pathway (usually the first irreversible step, called committed step), thus regulating the amount of end product made by the pathways.

  5. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    This can be seen as a consequence of Le Chatelier's principle because the inhibitor binds to both the enzyme and the enzyme-substrate complex equally so that the equilibrium is maintained. However, since some enzyme is always inhibited from converting the substrate to product, the effective enzyme concentration is lowered. Mathematically,

  6. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Competitive inhibition can be reversible or irreversible. If it is reversible inhibition, then effects of the inhibitor can be overcome by increasing substrate concentration. [8] If it is irreversible, the only way to overcome it is to produce more of the target (and typically degrade and/or excrete the irreversibly inhibited target).

  7. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    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.

  8. Product inhibition - Wikipedia

    en.wikipedia.org/wiki/Product_inhibition

    Product inhibition is a type of enzyme inhibition where the product of an enzyme reaction inhibits its production. [1] Cells utilize product inhibition to regulate of metabolism as a form of negative feedback controlling metabolic pathways. [2]

  9. Mixed inhibition - Wikipedia

    en.wikipedia.org/wiki/Mixed_inhibition

    a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]