The study of a large number of chemical reactions reveals that most do not go to true completion. This is likewise true of enzymatically-catalyzed reactions. This is due to the reversibility of most reactions.
where K+1 is the forward reaction rate constant and K-1 is the rate constant for the reverse reaction.
Combining the two reactions gives:
Applying this general relationship to enzymatic reactions allows the equation:
Equilbrium, a steady state condition, is reached when the forward reaction rates equal the backward rates. This is the basic equation upon which most enzyme activity studies are based.
Last modified: Thursday, 19 January 2012, 11:02 AM