Theoretical analysis of the significance of whether or not enzymes or transport systems in structured media follow Michaelis-Menten kinetics.
Pure Michaelis-Menten enzymes have been studied (i.e., enzymes with a hyperbolic (S, V) behavior in a well-stirred solution). When such enzymes are associated with a structure in vitro, even in the simplest conceivable form (immobilization in a homogeneous gel), they can produce enzymic or transport reactions with many different kinetics (Michaelis-Menten, sigmoidal, dual-phasic, etc.). Therefore, when structured enzyme or transport processes in vivo have sigmoidal kinetics, it is not proof that the corresponding proteins are allosteric. In same manner, when the apparent kinetics are dual-phasic, it is not proof that two enzyme, or transport systems, coexist.
D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological
D002352:Carrier Proteins; D004798:Enzymes