Michaelis constant: Difference between revisions
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Michaelis constant is the substrate concentration at which the reaction velocity is equal to half the maximal velocity of the reaction. | |||
K<sub>m</sub> = Michaelis constant | |||
K<sub>m</sub> = the value of substrate concentration[S] that causes V= ½ V<sub>max</sub> * | |||
The units of K<sub>m</sub> are M, [[Concentration|concentration]]. | |||
K<sub>m</sub> indicates the affinity of the enzyme for its substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]]. | |||
Velocity is related to K<sub>m </sub>through the Michaelis & Menten equation: v = (V<sub>max</sub> [S])/(K<sub>m</sub> + [S]). | |||
< | [[Vmax|V<sub>max</sub>]] = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration. | ||
= | [S] = [[Substrate|substrate]] concentration. | ||
<ref> | A reaction with a low Michaelis constant value indicates a low binding affinity, whereas a large value indicates a high binding affinity<ref>Michaelis, L; Menten, ML; Johnson, KA; Goody, R S. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper, | ||
Biochemistry, 04 October 2011, Vol.50(39), pp.8264-9</ref>. | |||
=== | === References<br> === | ||
<references /> | |||
< | |||
Latest revision as of 17:51, 6 December 2018
Michaelis constant is the substrate concentration at which the reaction velocity is equal to half the maximal velocity of the reaction.
Km = Michaelis constant
Km = the value of substrate concentration[S] that causes V= ½ Vmax *
The units of Km are M, concentration.
Km indicates the affinity of the enzyme for its substrate and thus the stability of the Enzyme-Substrate Complex.
Velocity is related to Km through the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S]).
Vmax = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration.
[S] = substrate concentration.
A reaction with a low Michaelis constant value indicates a low binding affinity, whereas a large value indicates a high binding affinity[1].
References
- ↑ Michaelis, L; Menten, ML; Johnson, KA; Goody, R S. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper, Biochemistry, 04 October 2011, Vol.50(39), pp.8264-9