Abstract
One can observe Michaelian kinetics in the case when the enzyme does not follow Michaelis-Menten mechanism and one can determine deviations from Michaelis-Menten kinetics with an enzyme that follows Michaelian mechanism. The discrepancies between the measured kinetics and real mechanism may be due to the existence of isoenzymes, the non-identical behaviour of subunits in oligomeric enzymes, the association-dissociation of oligomers, the instability of the enzyme under assay conditions, the effect of ligands, interaction with proteins, other macromolecules or membrances, etc.
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Keleti, T. (1981). Data Analysis from Michaelis-Menten Kinetics: Ins and Outs. In: Endrenyi, L. (eds) Kinetic Data Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3255-8_21
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