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It indicates that the enzyme has a high affinity for the substrate.
The Michaelis constant (Km) is a means of characterising an enzyme's affinity for a substrate. The Km in an enzymatic reaction is the substrate concentration at which the reaction rate is half its maximum speed. Thus, a low Km value means that the enzyme has a high affinity for the substrate (as a "little" substrate is enough to run the reaction at half its max speed). This is only true for reactions where substrate is limiting and the enzyme is NOT allosteric.
The Michaelis-Menten constant (Km) is calculated by determining the substrate concentration at half of the maximum reaction rate (Vmax). This value can be obtained by plotting reaction rates against substrate concentrations and identifying the point where the reaction rate is half of Vmax. Km represents the affinity of the enzyme for its substrate.
Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
It doesn't
It doesn't
the kinetic about substrate saturation (for example enzyme kinetics. it include Michaelis-Menten kinetic Hadiseh Rahmani
in an enzyme-substrate complex, the enzyme acts on the substrate .
enzyme-substrate complex
The binding of an enzyme and a substrate forms an enzyme-substrate complex. It lowers the activation energy of a chemical reaction
The lock and key model means that the substrate must perfectly fit the enzyme, and the enzyme does not change. The induced fit model is different as when the substrate fits together with the enzyme, the enzyme itself will change to either join substrates together or break a substrate down.
NO. The enzyme acts on the substrate. The substrate is the chemical/compound being altered by the action of the enzyme. They are NOT the same.