| Km | Michaelis-Menten constant |
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| Menten, Maud | <person> Canadian pathologist in U.S., 1879-1960. See: Michaelis-Menten constant, Michaelis-Menten hypothesis. (05 Mar 2000) |
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| Victor-Michaelis-Menten equation | <chemistry> Equation derived from a simple kinetic model for a single-substrate non-cooperative enzyme-catalyzed reaction that successfully accounts for the hyperbolic adsorption isotherm) relationship between substrate concentration and reaction rate. V = Vmax x S/(S + Km), where V is the initial velocity of the reaction, Km is the Michaelis constant, Vmax is the maximum rate approached by very high substrate concentrations and S is the initial substrate concentration. Similar equations can be derived for conditions in which the product is present and for multisubstrate enzymes. Synonym: Victor-Michaelis-Menten equation. (12 Jul 2000) |
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| Michaelis-Menten constant | <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. (05 Mar 2000) |
| Michaelis-Menten equation | <chemistry> Equation derived from a simple kinetic model for a single-substrate non-cooperative enzyme-catalyzed reaction that successfully accounts for the hyperbolic adsorption isotherm) relationship between substrate concentration and reaction rate. V = Vmax x S/(S + Km), where V is the initial velocity of the reaction, Km is the Michaelis constant, Vmax is the maximum rate approached by very high substrate concentrations and S is the initial substrate concentration. Similar equations can be derived for conditions in which the product is present and for multisubstrate enzymes. Synonym: Victor-Michaelis-Menten equation. (12 Jul 2000) |
| Michaelis-Menten hypothesis | <chemistry> That a complex is formed between an enzyme and its substrate (the O'Sullivan-Tompson hypothesis), which complex then decomposes to yield free enzyme and the reaction products (Brown hypothesis), the latter rate determining the overall rate of substrate-product conversion. See: Michaelis-Menten constant, Michaelis-Menten equation. (05 Mar 2000) |
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