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Passive transport in the interstitium and circulation: basics
Published in Benjamin Loret, Fernando M. F. Simões, Biomechanical Aspects of Soft Tissues, 2017
Benjamin Loret, Fernando M. F. Simões
The maximum rate of advancement Jmax ≡ k2+ [E]0 [unit : M/s] occurs when the enzyme is completely saturated with substrate, i.e. [A] ≫ Ka, and it is a characteristic of the efficiency of the catalysis. For [A] = Ka, J = Jmax/2: the Michaelis constant Ka indicates the affinity of the enzyme for the substrate. It is also the value of [A] for which half of the enzyme molecules binds to the substrate. The rate constant k2+ is sometimes noted kcat and termed turnover number as it represents the maximum number of substrate molecules that the enzyme can turn over to product per unit time. The rate of advancement at low concentration of substrate is governed by the specificity constantkcat/Ka. In practice, Ka and Jmax can be calculated by plotting J = Jmax − Ka J/[A] as a function of J/[A], so-called Eadie-Hofstee diagram.
Synthesis and characterization of a new 4-styrylpyridine based square planar copper(II) complex: exploration of phenoxazinone synthase-mimicking activity and DFT study
Published in Journal of Coordination Chemistry, 2019
Akhtaruz Zaman, Samim Khan, Basudeb Dutta, Sobhy M. Yakout, Shebl S. Ibrahim, Mohammad Hedayetullah Mir
All these enzyme kinetic plots have been used to evaluate several kinetic parameters, including turnover number (kcat) and specificity constant (kcat/KM) for phenoxazinone synthase-mimicking activity of the complex. In enzyme kinetics, turnover number (also termed as kcat) is defined as the maximum number of catalytic conversions of substrate molecules per unit of time that a single catalytic site will execute for a specific enzyme concentration. The specificity constant (also termed as kcat/KM ratio) is a measure of how efficiently a catalyst converts substrates into products. This ratio is a useful index for measuring the substrate specificity of catalyst. The higher the specificity constant, the more the enzyme prefers that substrate. Figures 5 and S2 represent the Michaelis–Menten plot, Lineweaver–Burk plot, Hanes–Woolf plot and Eadie–Hofstee plot for catalytic oxidation of OAPH in methanol and in 20% methanol, respectively. Tables 2 and S4 contain kinetic parameters for phenoxazinone synthase-mimicking activity in methanol and in 20% methanol, respectively.