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|enzyme]] reaction and is as follows:<br> | ||
=== V= Vmax[S]/Km[S] === | |||
V = is the rate of the reaction | |||
V<sub>max </sub>= is the maximal rate of the reaction | |||
K<sub>m </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 has for its substrate 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 /> | |||
<br> | |||
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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
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 1/2 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
- ↑ 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),