Michaelas Constant: Difference between revisions
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Michealas Constant (K<sub>m</sub> ) is the affinity between an enzyme and a substrate. It is the halfway point of V<sub>max</sub> , or V<sub>max</sub>/2. <sub></sub> | Michealas Constant (K<sub>m</sub> ) is the affinity between an enzyme and a substrate. It is the halfway point of [[Vmax|V<sub>max</sub>]] , or V<sub>max</sub>/2. <sub></sub> | ||
K<sub>m</sub> is inversely proportional to the affinity between an enzyme and a substrate. The higher the K<sub>m</sub>, the lower the affinity. <ref>↑ Berg J., Tymoczko J. and Stryer L. (2012) Biochemistry, 7th Edition, New York: W.H. Freeman.</ref> | K<sub>m</sub> is inversely proportional to the affinity between an enzyme and a substrate. The higher the K<sub>m</sub>, the lower the affinity. <ref>↑ Berg J., Tymoczko J. and Stryer L. (2012) Biochemistry, 7th Edition, New York: W.H. Freeman.</ref> | ||
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Revision as of 10:20, 28 November 2014
Michealas Constant (Km ) is the affinity between an enzyme and a substrate. It is the halfway point of Vmax , or Vmax/2.
Km is inversely proportional to the affinity between an enzyme and a substrate. The higher the Km, the lower the affinity. [1]
Reference
- ↑ ↑ Berg J., Tymoczko J. and Stryer L. (2012) Biochemistry, 7th Edition, New York: W.H. Freeman.