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 ?
Presence of time hierarchy makes possible the saturated response of the output to the WIP in the form of the Karmarkar clearing function (in fact the Michaelis-Menten equation), whereas the side buffer leakage secures finiteness of the steady-state inventory level.
The relationship between the reciprocal of the response current ([i.sup.-1]) and the reciprocal of the lactose concentration ([C.sup.-1]) was obtained according to the Lineweaver-Burk form of the Michaelis-Menten equation (Figure 9) [64].
Kinetics properties of L.plantarum uricase were determined using Michaelis-Menten equation and Lineweaver-Burk plot, where:
Ever-fluctuating single enzyme molecules: Michaelis-Menten equation revisited.
The kinetic parameters of [alpha]-glucosidase inhibitory protein were determined by using LineweaverBurk plots (22) and Michaelis-Menten equation and its reciprocal.
Two different substrate concentrations were chosen to explain enzyme kinetics, using the Michaelis-Menten equation. With two values for initial velocities and substrate concentrations, [V.sub.max] and [K.sub.m] values of the reactions could be established (Figure 8).
The Lineweaver-Burk equation canbe derived from the Michaelis-Menten equation:
The curve which expresses the relationship between substrate concentration and initial velocity has the same shape for most enzymes, a rectangular hyperbola, whose algebraic expression is given by Michaelis-Menten equation (1), which describes the relationship between initial velocity [V.sub.o] and substrate concentration, S [1]:
Kinetic parameters were determined by fitting the data to the Michaelis-Menten equation using GraFit [24].
As well known, the electrical response of an amperometric biosensor is well described by Michaelis-Menten equation:
The model used for ChiA from Serratia marcescens (Equation 1) fit satisfactorily to the experimental data with colloidal chitin, while for 4-MUF kinetics the Michaelis-Menten equation for substrate inhibition fit better (Figure 6B).