In <9401111729.AA09031 at net.bio.net>
mroussel at alchemy.chem.utoronto.ca (Marc Roussel) writes:
> There are few tables of equilibrium constants. Instead, use tables
>of Gibbs free energies of formation.
[snip]
A single enzyme is capable of taking a reaction essentially to completion,
far from thermodynamic equilibrium. If the enzymes for both a forward and
reverse reaction are operating simultaneously, then one can expect a
steady state, or "dynamic equilibrium" to be achieved, but is this necessarily
the same as the thermodynamic equilibrium? Won't it be changed by changing
the relative amounts of the forward and reverse enzyme? (At the limit when
one of the two is completely removed, one should return to the essentially
irreversible case.) And if this is true, how applicable is the thermodynamic
equil. constant to computing the relative levels of the compunds *in vivo*?
Paul
schlosser at beta.ciit.org
