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> = Michaelis constant  


K<sub>m</sub> = the value of [S] that causes V= ½ V<sub>max</sub> *  
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]].  
The units of K<sub>m</sub> are M, [[Concentration|concentration]].  


K<sub>m</sub> indicates the [[javascript:void(0);/*1512127072657*/|affinity]] of the enzyme for its substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]].  
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 &amp; 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.  


High K<sub>m</sub> demonstrates a low affinity; Low Km demonstrates a high affinity.  
[S] = [[Substrate|substrate]] concentration.  


Velocity is related to K<sub>m&nbsp;</sub>through the Michaelis &amp; Menten equation:&nbsp;v = (V<sub>max</sub> [S])/(K<sub>m</sub> + [S]).<br>
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>.  


*[[Vmax|V<sub>max</sub>]] = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration.
=== References<br> ===


[S] = [[Substrate|substrate]] concentration.<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

  1. ↑ 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
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