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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. 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.

  4. 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.

  5. 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 ...

  6. 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).

  7. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    While the Lineweaver–Burk plot has historically been used for evaluation of the parameters, together with the alternative linear forms of the Michaelis–Menten equation such as the Hanes–Woolf plot or Eadie–Hofstee plot, all linearized forms of the Michaelis–Menten equation should be avoided to calculate the kinetic parameters ...

  8. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    In the Arrhenius model of reaction rates, activation energy is the minimum amount of energy that must be available to reactants for a chemical reaction to occur. [1] The activation energy ( E a ) of a reaction is measured in kilojoules per mole (kJ/mol) or kilocalories per mole (kcal/mol). [ 2 ]

  9. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    = Rate of the reaction = Reaction volume. The SI unit is the katal, 1 katal = 1 mol s −1 (mole per second), but this is an excessively large unit. A more practical and commonly used value is enzyme unit (U) = 1 μmol min −1 (micromole per minute). 1 U corresponds to 16.67 nanokatals. [1]