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K<sub>m</sub>, or [[Michaelis constant|Michaelis constant]] indicates the affinity of an enzyme for its substrate. In other words, how stable the [[enzyme|enzyme]] substrate complex is. It can be found by plotting velocity against substrate concentration of an enzyme catalysed reaction. K<sub>m</sub> = to [[Vmax|Vmax]]/2. A high Km value displays a low affinity and a low K<sub>m</sub> value displays a high affinity. The units of K<sub>m</sub> are molarity (M) <ref>Worthington Biochem, 2011, available online at http://www.worthington-biochem.com/introbiochem/substrateconc.html (last accessed 02/12/2011)</ref><ref>U.K answers, 2008, available online at http://uk.answers.yahoo.com/question/index?qid=20071126082146AA0R5W2 (last accessed 02/12/2011)</ref>. | |||
Also see [[Michaelis_menten_equation|Michaelis menten equation]] | |||
=== References === | |||
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Latest revision as of 17:13, 2 December 2011
Km, or Michaelis constant indicates the affinity of an enzyme for its substrate. In other words, how stable the enzyme substrate complex is. It can be found by plotting velocity against substrate concentration of an enzyme catalysed reaction. Km = to Vmax/2. A high Km value displays a low affinity and a low Km value displays a high affinity. The units of Km are molarity (M) [1][2].
Also see Michaelis menten equation
References
- ↑ Worthington Biochem, 2011, available online at http://www.worthington-biochem.com/introbiochem/substrateconc.html (last accessed 02/12/2011)
- ↑ U.K answers, 2008, available online at http://uk.answers.yahoo.com/question/index?qid=20071126082146AA0R5W2 (last accessed 02/12/2011)