Michaelis-Menten constant: Difference between revisions

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K<sub>m&nbsp;</sub>= the concentration at which V<sub>max</sub> is 1/2<br>  
K<sub>m&nbsp;</sub>= the concentration at which V<sub>max</sub> is 1/2<br>  


Using the K<sub>m</sub>, this equation is useful to tell the affinity an enzyme has for its substrate. If the K<sub>m</sub> is high, this means the concentration at which 1/2 V<sub>max</sub> is reached is high, so the affinity the enzyme&nbsp;has for its substrate&nbsp;is low (because a lot of substrate is needed to reach 1/2 V<sub>max</sub>). If K<sub>m</sub> is low, this means the affinity is high, because less substrate was needed to get to half the maximal rate of the reaction (V<sub>max</sub>) <ref>Down, J.E and Riggs, D.S. 1965, A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations. The Journal of Biological chemistry. 240 (2),</ref>.  
Using the K<sub>m</sub>, this equation is useful to tell the affinity an enzyme has for its substrate. If the K<sub>m</sub> is high, this means the concentration at which 1/2 V<sub>max</sub> is reached is high, so the affinity the enzyme&nbsp;has for its substrate&nbsp;is low (because a lot of substrate is needed to reach 1/2 V<sub>max</sub>). If K<sub>m</sub> is low, this means the affinity is high, because less substrate was needed to get to half the maximal rate of the reaction (V<sub>max</sub>)<ref>Down, J.E and Riggs, D.S. 1965, A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations. The Journal of Biological chemistry. 240 (2),</ref>.  


=== References ===
=== References ===


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<references />  


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Latest revision as of 16:19, 5 December 2018

The Michaelis-Menten describes and enzyme reaction and is as follows:

V= Vmax[S]/Km[S]

V = is the rate of the reaction

Vmax = is the maximal rate of the reaction

K= the concentration at which Vmax is 1/2

Using the Km, this equation is useful to tell the affinity an enzyme has for its substrate. If the Km is high, this means the concentration at which 1/2 Vmax is reached is high, so the affinity the enzyme has for its substrate is low (because a lot of substrate is needed to reach 1/2 Vmax). If Km is low, this means the affinity is high, because less substrate was needed to get to half the maximal rate of the reaction (Vmax)[1].

References

  1. Down, J.E and Riggs, D.S. 1965, A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations. The Journal of Biological chemistry. 240 (2),