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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. Glutamine synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutamine_synthetase

    Glutamate is another product of glutamine metabolism; however, glutamate is a substrate for GS inhibiting it to act as a regulator to GS.2 Each inhibitor can reduce the activity of the enzyme; once all final glutamine metabolites are bound to GS, the activity of GS is almost completely inhibited. [8]

  4. Linear biochemical pathway - Wikipedia

    en.wikipedia.org/wiki/Linear_biochemical_pathway

    Linear pathways follow a step-by-step sequence, where each enzymatic reaction results in the transformation of a substrate into an intermediate product. This intermediate is processed by subsequent enzymes until the final product is synthesized. A linear chain of four enzyme-catalyzed steps. A linear pathway can be studied in various ways.

  5. Fructose 1,6-bisphosphatase - Wikipedia

    en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase

    Fructose 1,6-bisphosphate aldolase is another temperature dependent enzyme that plays an important role in the regulation of glycolysis and gluconeogenesis during hibernation. [14] Its main role is in glycolysis instead of gluconeogenesis, but its substrate is the same as FBPase's, so its activity affects that of FBPase in gluconeogenesis.

  6. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Daniel Koshland's theory of enzyme-substrate binding is that the active site and the binding portion of the substrate are not exactly complementary. [10] The induced fit model is a development of the lock-and-key model and assumes that an active site is flexible and changes shape until the substrate is completely bound.

  7. Aspartate carbamoyltransferase - Wikipedia

    en.wikipedia.org/wiki/Aspartate_carbamoyltransferase

    Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2). [1]In E. coli, the enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total). [2]

  8. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes. [1]: 26 In most cases of a metabolic pathway, the product of one enzyme acts as the substrate for the next. However, side products are considered waste and removed from the cell.

  9. 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.