Steady-state kinetic behaviour of two- or n-enzyme systems made of free sequential enzymes involved in a metabolic pathway.
The overall rate of functioning of a set of free sequential enzymes of the Michaelis-Menten type involved in a metabolic pathway has been computed as a function of the concentration of the initial substrate under steady-state conditions. Curves monotonically increasing up to a saturation plateau have been obtained in all cases. The shape of these curves is sometimes, but not usually, close to that of a hyperbola. Cases exist in which the overall rate of reaction becomes quasi proportional to the concentration of initial substrate almost up to the saturation plateau, which never occurs with individual enzymes. Increasing the number of enzymes sequentially involved in a metabolic pathway does not seem to generate any particularly original behaviour compared with that of two-enzyme systems.
Legent
Guillaume
G
Laboratoire Assemblages Moléculaire : Modélisation et Imagerie SIMS), FRE CNRS 2829, Faculté des Sciences de l'Université de Rouen, 76821 Mont-Saint-Aignan cedex, France. g_legent@hotmail.com
Thellier
Michel
M
Norris
Vic
V
Ripoll
Camille
C
D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008962:Models, Theoretical; D015398:Signal Transduction
D004798:Enzymes