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In chemistry, the term "turnover number" has two distinct meanings.. 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]
Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.
Michaelis–Menten kinetics have also been applied to a variety of topics outside of biochemical reactions, [14] including alveolar clearance of dusts, [19] the richness of species pools, [20] clearance of blood alcohol, [21] the photosynthesis-irradiance relationship, and bacterial phage infection. [22]
The common form of the inhibitory term also obscures the relationship between the inhibitor binding to the enzyme and its relationship to any other binding term be it the Michaelis–Menten equation or a dose response curve associated with ligand receptor binding. To demonstrate the relationship the following rearrangement can be made:
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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 ...
a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]
When a non-competitive inhibitor is added the Vmax is changed, while the Km remains unchanged. According to the Lineweaver-Burk plot the Vmax is reduced during the addition of a non-competitive inhibitor, which is shown in the plot by a change in both the slope and y-intercept when a non-competitive inhibitor is added. [8]