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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. 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.

  4. Secondary plot (kinetics) - Wikipedia

    en.wikipedia.org/wiki/Secondary_plot_(kinetics)

    In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver–Burk plots to find additional kinetic constants. [1] [2]For example, when a set of v by [S] curves from an enzyme with a ping–pong mechanism (varying substrate A, fixed substrate B) are plotted in a Lineweaver–Burk plot, a set of parallel lines will be produced.

  5. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    On a Lineweaver-Burk plot, the presence of a noncompetitive inhibitor is illustrated by a change in the y-intercept, defined as 1/V max. The x-intercept, defined as −1/K M, will remain the same. In competitive inhibition, the inhibitor will bind to an enzyme at the active site, competing with the substrate.

  6. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  7. Enzyme Commission number - Wikipedia

    en.wikipedia.org/wiki/Enzyme_Commission_number

    The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. [1] As a system of enzyme nomenclature , every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction.

  8. Phosphoinositide phospholipase C - Wikipedia

    en.wikipedia.org/wiki/Phosphoinositide_phospho...

    These enzymes belong to a larger superfamily of Phospholipase C. Other families of phospholipase C enzymes have been identified in bacteria and trypanosomes. Phospholipases C are phosphodiesterases. Phospholipase Cs participate in phosphatidylinositol 4,5-bisphosphate (PIP 2) metabolism and lipid signaling pathways in a calcium-dependent manner.

  9. 4-aminobutyrate transaminase - Wikipedia

    en.wikipedia.org/wiki/4-aminobutyrate_transaminase

    In enzymology, 4-aminobutyrate transaminase (EC 2.6.1.19), also called GABA transaminase or 4-aminobutyrate aminotransferase, or GABA-T, is an enzyme that catalyzes the chemical reaction: 4-aminobutanoate + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } succinate semialdehyde + L-glutamate

  1. Related searches identify the enzyme labeled 4 in x and y intercept of 2x 6y 18 in two

    identify the enzyme labeled 4 in x and y intercept of 2x 6y 18 in two variables