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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. Eadie–Hofstee diagram - Wikipedia

    en.wikipedia.org/wiki/Eadie–Hofstee_diagram

    The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...

  4. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    An example of a coupled reaction is the phosphorylation of fructose-6-phosphate to form the intermediate fructose-1,6-bisphosphate by the enzyme phosphofructokinase accompanied by the hydrolysis of ATP in the pathway of glycolysis. The resulting chemical reaction within the metabolic pathway is highly thermodynamically favorable and, as a ...

  5. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.

  6. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, = + in which the rate is a function of the substrate concentration and two parameters , the limiting rate, and , the Michaelis constant.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis–Menten constant (K m), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic K M for a given substrate.

  8. Template:Enzymatic reaction - Wikipedia

    en.wikipedia.org/wiki/Template:Enzymatic_reaction

    See a monthly parameter usage report for Template:Enzymatic reaction in articles based on its TemplateData. TemplateData for Enzymatic reaction This template should be used on enzyme pages to show the reactions that are produced and used by the enzyme, especially when part of a major biochemical pathway such as glycolysis.

  9. Reversible Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Reversible_Michaelis...

    Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics. The rate of reaction of many chemical reactions shows a linear response as function of the concentration of substrate molecules.