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  2. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In chemistry, the term "turnover number" has two distinct meanings.. In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1]

  3. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.

  4. 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 ...

  5. Specificity constant - Wikipedia

    en.wikipedia.org/wiki/Specificity_constant

    In the field of biochemistry, the specificity constant (also called kinetic efficiency or /), is a measure of how efficiently an enzyme converts substrates into products.A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity).

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    As larger amounts of substrate are added to a reaction, the available enzyme binding sites become filled to the limit of .Beyond this limit the enzyme is saturated with substrate and the reaction rate ceases to increase.

  7. 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.

  8. Rate-limiting step (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Rate-limiting_step...

    Webb (1963) [9] was highly critical of the concept of the rate-limiting step and of its blind application to solving problems of regulation in metabolism. Waley (1964) [ 10 ] made a simple but illuminating analysis of simple linear chains.

  9. Katal - Wikipedia

    en.wikipedia.org/wiki/Katal

    The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.