Michaelis-Menten constant: Difference between revisions
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The Michaelis-Menten describes and enzyme reaction and is as follows: | The Michaelis-Menten describes and enzyme reaction and is as follows: | ||
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=== V= Vmax[S]/Km[S] === | |||
V= is the rate of the reaction | |||
Vmax= is the maximal rate of the reaction | |||
Km= the concentration at which Vmax is 1/2 | |||
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Vmax | 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 1/2Vmax 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). | ||
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), | |||
Revision as of 11:18, 16 October 2014
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
Km= 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 1/2Vmax 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).
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),