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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. Like other catalysts, enzymes do not alter the position of equilibrium between substrates and products. [1] However, unlike uncatalysed chemical reactions, enzyme-catalysed reactions display saturation kinetics.

  3. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    An illustration to show (a) Alberty-Hammes-Eigen model, and (b) Chou's model, where E denotes the enzyme whose active site is colored in red, while the substrate S in blue. The theory of diffusion-controlled reaction was originally utilized by R.A. Alberty, Gordon Hammes, and Manfred Eigen to estimate the upper limit of enzyme-substrate reaction.

  4. 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.

  5. Chemical kinetics - Wikipedia

    en.wikipedia.org/wiki/Chemical_kinetics

    In autocatalysis a reaction product is itself a catalyst for that reaction leading to positive feedback. Proteins that act as catalysts in biochemical reactions are called enzymes. Michaelis–Menten kinetics describe the rate of enzyme mediated reactions. A catalyst does not affect the position of the equilibrium, as the catalyst speeds up the ...

  6. Regulatory enzyme - Wikipedia

    en.wikipedia.org/wiki/Regulatory_enzyme

    Regulatory enzymes are commonly the first enzyme in a multienzyme system: the product of the reaction catalyzed by the first enzyme is the substrate of the second enzyme, so the cell can control the amount of resulting product by regulating the activity of the first enzyme of the pathway.

  7. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by ...

  8. Catalysis - Wikipedia

    en.wikipedia.org/wiki/Catalysis

    Several factors affect the activity of enzymes (and other catalysts) including temperature, pH, the concentration of enzymes, substrate, and products. A particularly important reagent in enzymatic reactions is water, which is the product of many bond-forming reactions and a reactant in many bond-breaking processes.

  9. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.