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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated.

  3. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]

  4. Eadie–Hofstee diagram - Wikipedia

    en.wikipedia.org/wiki/Eadie–Hofstee_diagram

    Eadie–Hofstee plot of v against v/a for Michaelis–Menten kinetics. In biochemistry, an Eadie–Hofstee plot (or Eadie–Hofstee diagram) is a graphical representation of the Michaelis–Menten equation in enzyme kinetics. It has been known by various different names, including Eadie plot, Hofstee plot and Augustinsson plot.

  5. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    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] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]

  6. Reversible Michaelis–Menten kinetics - Wikipedia

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

    Reversible Michaelis–Menten kinetics, using the reversible form of the Michaelis–Menten equation, is therefore important when developing computer models of cellular processes involving enzymes. In enzyme kinetics, the Michaelis–Menten kinetics kinetic rate law that describes the conversion of one substrate to one product, is often ...

  7. Hill equation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Hill_equation_(biochemistry)

    Noncooperative (completely independent) binding: The affinity of the enzyme for a ligand molecule is not dependent on whether or not other ligand molecules are already bound. When n=1, we obtain a model that can be modeled by Michaelis–Menten kinetics , [ 11 ] in which K D = K A = K M {\textstyle K_{D}=K_{A}=K_{M}} , the Michaelis–Menten ...

  8. Hanes–Woolf plot - Wikipedia

    en.wikipedia.org/wiki/Hanes–Woolf_plot

    Hanes plot of a/v against a for Michaelis–Menten kinetics In biochemistry , a Hanes–Woolf plot , Hanes plot , or plot of a / v {\displaystyle a/v} against a {\displaystyle a} is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration a {\displaystyle a} to the reaction velocity v ...

  9. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...