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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 ...
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 ...
In biochemistry, a Hanes–Woolf plot, Hanes plot, or plot of / against is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration to the reaction velocity is plotted against .
The analysis of these reactions is much simpler if the concentration of substrate A is kept constant and substrate B varied. Under these conditions, the enzyme behaves just like a single-substrate enzyme and a plot of v by [S] gives apparent K M and V max constants for substrate B. If a set of these measurements is performed at different fixed ...
The best known plots of the Michaelis–Menten equation, including the double-reciprocal plot of / against /, [2] the Hanes plot of / against , [3] and the Eadie–Hofstee plot [4] [5] of against / are all plots in observation space, with each observation represented by a point, and the parameters determined from the slope and intercepts of the lines that result.
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.
Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.
It can be recognized by two observations: first, it cannot be reversed by increasing the substrate concentration , and second, linear plots show effects on and , seen, for example, in the Lineweaver–Burk plot as parallel rather than intersecting lines. It is sometimes explained by supposing that the inhibitor can bind to the enzyme-substrate ...