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Michaelis-menten constant

Michaelis-Menten constant –>
Michaelis constant
(Science: chemistry) The true dissociation constant for the enzymesubstrate binary complex in a single-substrate rapid equilibrium enzyme-catalyzed reaction (usually symbolised by Ks), the concentration of the substrate at which half the true maximum velocity of an enzyme-catalyzed reaction is achieved (when velocities are measured under initial rate and steady state conditions).
The ratio of rate constants (k2 – k3)/k1 in the singlesubstrate enzyme-catalyzed reaction: E – S &dblarr; eS &dblarr; E – products where E represents the free enzyme, S is the substrate, and ES is the central binary complex. The expression for the michaelis constant will be more complex for multisubstrate reactions.
An apparent michaelis constant is a constant determined either under conditions that are not strictly steady state and initial rate or one that varies with the concentration of one or more cosubstrates.
See: michaelis-Menten equation.
Synonym: michaelis-Menten constant.


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