Michaelis-Menten equation


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Michaelis-Menten equation

[‚mik·ä¦ā·ləs ′men·tən i‚kwā·zhən]
(biochemistry)
A mathematical equation expressing the hyperbolic relationship between the initial velocity, Vo , and the substrate concentration, [S ], in a number of enzyme-catalyzed reactions such that Vo = Vmax[S ]/ Km + [S ], where Vmaxis the maximum velocity and Km is the Michaelis constant.
References in periodicals archive ?
In 2009, Grima used mathematical models and computer simulations to show that two basic assumptions behind the Michaelis-Menten equation throw its predictions off in real cells.
This variation could also mean that even if one cell follows the Michaelis-Menten equation, large groups of cells taken all together might not, Kim says.
The accurate fit of the data to the Michaelis-Menten equation provides a good test for the simple apparatus used.
The mean rate of conversion was plotted vs the mean substrate concentration at the chosen time interval (20), and the results were directly fitted to the Michaelis-Menten equation.
Fitting the data on concentration dependency with the Michaelis-Menten equation (Fig.
Taking into consideration that the kinetics of denitrification is based on enzyme activity, the rate equation describing the process by activated sludge can be based on the Michaelis-Menten equation for the two substrate process.
This resulted in the Michaelis-Menten equation, a basic biochemical concept that brought them international recognition.
Generalized Michaelis-Menten Equation for Conformation Modulated Monomeric Enzymes
Then, for each trial, the initial velocity of ClpB was plotted versus the final concentration of ATP; and the data set was fit using nonlinear regression according to the Michaelis-Menten equation.