Update
[May 2015]
 A significantly enhanced version of this online tool
was made part of the software package DynaFit.
 See BioKin Technical Note TN201503 for details.
Theory
By design, this online tool derives the final rate equation in the same
general form as is shown in Equation IX181 (Bi Uni Random mechanism) on page 647 in Segel's Enzyme Kinetics:
In other words, no attempt is made to further manipulate groups of rate constants
(K_{1}, K_{2}, K_{3}, etc.) in order
to produce Michaelis constants and inhibition constants.
The reason for this is given on page 647 in Segel's book:
"The equation does not describe a hyperbola and, theoretically, the reciprocal plots are not linear,
unless one substrate is saturating. [...] The groups of rate constants cannot be combined into
convenient kinetic constants [Michaelis constants and inhibition constants]."
This also true for the Bi Bi Random mechanism (Segel, p. 649) and other relatively complex branched mechanisms.
In all these cases the Michaelis constants cannot be defined either formally or phenomenologically
("concentration of substrate at which halfsaturating reaction rate is reached").
Indeed, the substrate saturation curve in these complex cases is not a rectangular hyperbola, and for this reason it does not
make sense to speak about "halfmaximum velocity", at least not in the same sense that is applicable to the simple MichaelisMenten mechanism.
In fact, Segel (p. 659) gives a nice overview of the great variety of substrate saturations curves that arise in the case of the Bi Bi Random
mechanism, depending on the relationship between the values of elementary rate constants. The illustrations in Segel's Figure IX37 include the following cases of nonhyperbolic kinetics:
 sigmoidal saturation curves;
 saturation curves with local maxima;
 sigmoidal saturation curves with local maxima;
 nonhyperbolic curves without sigmoidal onset or local maxima.
Thus, in the most general case of multisubstrate kinetics, it is not possible
to group elementary rate constants to arrive at K_{M} and K_{i} values.
