Michaelis menten equation: Difference between revisions

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'''V'''<sub>'''max'''</sub> is the maximum rate of an enzyme reaction, occurs when all substrate is saturated.<br>  
'''V'''<sub>'''max'''</sub> is the maximum rate of an enzyme reaction, occurs when all substrate is saturated.<br>  


'''K<sub>m</sub>''' is the Michaelis-Menten constant and is the substrate concentration at half V<sub>max.&nbsp;</sub>  
'''K<sub>m</sub>''' is the Michaelis-Menten constant and is the substrate concentration at half V<sub>max.&nbsp;</sub><br>  


<br>  
<sub></sub>V<sub>max</sub> and K<sub>m</sub> can&nbsp;also be&nbsp;shown on a graph, the&nbsp;graph which shows this best is a&nbsp;'''double&nbsp;reciprocal plot'''.&nbsp;You can&nbsp;obtain&nbsp;the results&nbsp;by plotting 1/V against 1/[S]&nbsp;<ref>Molecular Biology of the Cell, Alberts et al., 5th Edition (2007) Garland Science, New York Chapter 3 p162-163</ref>.


<sub></sub>V<sub>max</sub> and K<sub>m</sub> can&nbsp;also be&nbsp;shown on a graph, the&nbsp;graph which shows this best is a&nbsp;'''double&nbsp;reciprocal plot'''.&nbsp;You can&nbsp;obtain&nbsp;the results&nbsp;by plotting 1/V against 1/[S]&nbsp;<ref>Molecular Biology of the Cell, Alberts et al., 5th Edition (2007) Garland Science, New York Chapter 3 p162-163</ref>.
=== References ===
 
=== References ===


<references />
<references />

Revision as of 18:25, 14 November 2010

The Michaelis-Menten equation is used to work out the rate of enzyme reactions and is written as follows:

                                                     V = Vmax [S]

                                                           Km + [S]

Vmax is the maximum rate of an enzyme reaction, occurs when all substrate is saturated.

Km is the Michaelis-Menten constant and is the substrate concentration at half Vmax. 

Vmax and Km can also be shown on a graph, the graph which shows this best is a double reciprocal plot. You can obtain the results by plotting 1/V against 1/[S] [1].

References

  1. Molecular Biology of the Cell, Alberts et al., 5th Edition (2007) Garland Science, New York Chapter 3 p162-163