Michaelas Constant

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&nbsp;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>]]&nbsp;, or V<sub>max</sub>/2.&nbsp;<sub></sub>  
 
&nbsp;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>]]&nbsp;, or V<sub>max</sub>/2.&nbsp;<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.&nbsp;<ref>Berg J., Tymoczko J. and Stryer L. (2012) Biochemistry, 7th Edition, New York: W.H. Freeman.</ref>  
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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.&nbsp;<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 11:22, 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

  1. Berg J., Tymoczko J. and Stryer L. (2012) Biochemistry, 7th Edition, New York: W.H. Freeman.
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