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Michaelis-menten constant

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Michaelis-Menten constant --> Michaelis constant

(Science: chemistry) The true dissociation constant for the enzyme-substrate 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 single-substrate 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.