# Michaelis menten equation

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'''V'''<sub>'''max'''</sub> is the maximum rate of an [[Enzyme|enzyme]] reaction, occurs when all substrate is saturated.<br> | '''V'''<sub>'''max'''</sub> is the maximum rate of an [[Enzyme|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 </sub>.<br> | + | '''K<sub>m</sub>''' is the Michaelis-Menten constant and is the substrate concentration at half V<sub>max </sub>. (Higher the Km value, lower the affinity)<br> |

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

## Latest revision as of 10:36, 22 October 2014

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

** V = V_{max} [S]**

** K _{m} + [S]**

**V**_{max} is the maximum rate of an enzyme reaction, occurs when all substrate is saturated.

**K _{m}** is the Michaelis-Menten constant and is the substrate concentration at half V

_{max }. (Higher the Km value, lower the affinity)

_{}V_{max} and K_{m} can also be shown on a graph, the graph which shows this best is a **double reciprocal plot **(Lineweaver-Burk plot). You can obtain the results by plotting 1/V against 1/[S] ^{[1]}.

### References

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