Michaelis constant: Difference between revisions
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K<sub>m</sub> = Michaelis constant | |||
K<sub>m</sub> = the value of [S] that causes V= ½ V<sub>max</sub> * | |||
The units of | The units of K<sub>m</sub> are M, concentration | ||
K<sub>m</sub> indicates the affinity of the enzyme for it's substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]]. | |||
High | High K<sub>m</sub> demonstrates a low affinity; Low Km demonstrates a high affinity. | ||
velocity is related to | velocity is related to K<sub>m </sub>through the Michaelis & Menten equation: v = (V<sub>max</sub> [S])/(K<sub>m</sub> + [S])<br> | ||
< | *V<sub>max</sub> = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration | ||
[S] = substrate concentration | [S] = substrate concentration | ||
Revision as of 16:24, 29 November 2012
Km = Michaelis constant
Km = the value of [S] that causes V= ½ Vmax *
The units of Km are M, concentration
Km indicates the affinity of the enzyme for it's substrate and thus the stability of the Enzyme-Substrate Complex.
High Km demonstrates a low affinity; Low Km demonstrates a high affinity.
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