# Michaelis constant

(Difference between revisions)
 Revision as of 17:22, 30 November 2012 (view source)Nnjm2 (Talk | contribs)← Older edit Revision as of 19:34, 30 November 2015 (view source)Newer edit → Line 1: Line 1: − Km = Michaelis constant + Km = Michaelis constant Km = the value of [S] that causes V= ½ Vmax * Km = the value of [S] that causes V= ½ Vmax * Line 5: Line 5: The units of Km are M, concentration The units of Km are M, concentration − Km indicates the affinity of the enzyme for it's substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]]. + Km indicates the affinity of the enzyme for its substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]]. High Km demonstrates a low affinity; Low Km demonstrates a high affinity. High Km demonstrates a low affinity; Low Km demonstrates a high affinity. − velocity is related to Kthrough the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S])
+ Velocity is related to Kthrough the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S])
*Vmax = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration *Vmax = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration [S] = substrate concentration
[S] = substrate concentration

## Revision as of 19:34, 30 November 2015

Km = Michaelis constant

Km = the value of [S] that causes V= ½ Vmax *

The units of Km are M, concentration

Km indicates the affinity of the enzyme for its substrate and thus the stability of the Enzyme-Substrate Complex.

High Km demonstrates a low affinity; Low Km demonstrates a high affinity.

Velocity is related to Kthrough the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S])

• Vmax = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration

[S] = substrate concentration