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  2. 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 ...

  3. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Determining the parameters of the Michaelis–Menten equation typically involves running a series of enzyme assays at varying substrate concentrations , and measuring the initial reaction rates , i.e. the reaction rates are measured after a time period short enough for it to be assumed that the enzyme-substrate complex has formed, but that the ...

  4. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    Effects of different types of inhibition on the double-reciprocal plot. When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish between competitive, pure non-competitive and uncompetitive inhibitors. The various modes of inhibition can be compared to the uninhibited reaction.

  5. 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.

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.

  7. Substrate inhibition in bioreactors - Wikipedia

    en.wikipedia.org/wiki/Substrate_inhibition_in...

    Substrate inhibition in bioreactors occurs when the concentration of substrate (such as glucose, salts, or phenols [1]) exceeds the optimal parameters and reduces the growth rate of the cells within the bioreactor. This is often confused with substrate limitation, which describes environments in which cell growth is limited due to of low substrate.

  8. Uncompetitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Uncompetitive_inhibition

    It can be recognized by two observations: first, it cannot be reversed by increasing the substrate concentration , and second, linear plots show effects on and , seen, for example, in the Lineweaver–Burk plot as parallel rather than intersecting lines. It is sometimes explained by supposing that the inhibitor can bind to the enzyme-substrate ...

  9. Hanes–Woolf plot - Wikipedia

    en.wikipedia.org/wiki/Hanes–Woolf_plot

    In biochemistry, a Hanes–Woolf plot, Hanes plot, or plot of / against is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration to the reaction velocity is plotted against .