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Two rules of enzyme kinetics for reversible Michaelis‐Menten mechanisms
Author(s) -
Keleti T.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81542-3
Subject(s) - kinetics , michaelis–menten kinetics , thermodynamics , chemistry , equilibrium constant , reversible reaction , steady state (chemistry) , substrate (aquarium) , enzyme kinetics , thermodynamic equilibrium , chemical equilibrium , product inhibition , chemical kinetics , reaction rate constant , dynamic equilibrium , rate equation , reaction rate , enzyme , catalysis , non competitive inhibition , physics , organic chemistry , active site , enzyme assay , classical mechanics , oceanography , geology
In a Michaelis‐Menten type reversible enzyme reaction (one substrate, one product) the rapid equilibrium kinetics in one direction excludes rapid equilibrium in the reverse direction. If rapid equilibrium functions in any direction, in the reverse reaction van Slyke type ‘kinetic constant’ appears in the rate equation independently of whether steady state is reached in finite time or the final equilibrium is attained at t = ∞ . If the reaction proceeds in one direction with rapid equilibrium and in the reverse direction with steady‐state kinetics, the thermodynamic equilibrium of the reaction determines that a higher equilibrium concentration of product (or substrate) can be reached only with steady‐state kinetics.