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  2. 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.

  3. 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 ...

  4. 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 ...

  5. Hill equation (biochemistry) - Wikipedia

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

    Each curve corresponds to a different Hill coefficient, labeled to the curve's right. The vertical axis displays the proportion of the total number of receptors that have been bound by a ligand. The horizontal axis is the concentration of the ligand. As the Hill coefficient is increased, the saturation curve becomes steeper.

  6. Propionyl-CoA carboxylase - Wikipedia

    en.wikipedia.org/wiki/Propionyl-CoA_carboxylase

    The native enzyme to biotin ratio has been determined to be one mole native enzyme to 4 moles biotin. [3] The N1 of biotin is thought to be the active site base. [4] Site-directed mutagenesis at D422 shows a change in the substrate specificity of the propionyl-CoA binding site, thus indicating this residue's importance in PCC's catalytic ...

  7. UDP-glucose 4-epimerase - Wikipedia

    en.wikipedia.org/wiki/UDP-glucose_4-epimerase

    The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose . [ 1 ]

  8. Today's Wordle Hint, Answer for #1256 on Tuesday, November 26 ...

    www.aol.com/lifestyle/todays-wordle-hint-answer...

    If you’re stuck on today’s Wordle answer, we’re here to help—but beware of spoilers for Wordle 1256 ahead. Let's start with a few hints.

  9. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.