The perfection of substrate-channelling in interacting enzyme systems: energetics and evolution.
Some implications of substrate channelling in interacting enzyme systems are considered, with regard to the energetics and evolution of enzyme action. The transient time, a key analytical parameter relating to the phenomenon of channelling, is the basis of our kinetic study. Bounds on the kinetics of multienzyme complexes are established using (apparent) rate constants emanating from the transient-time formulation of coupled reactions. From a transition state representation of the rate process, it is shown how dynamically and statically organized enzyme systems lead to the modification of current ideas on the evolutionary optimization of the energy profile of enzyme catalysis in situ.
Keleti
T
T
Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.
Vértessy
B
B
Welch
G R
GR
D005075:Biological Evolution; D002384:Catalysis; D004734:Energy Metabolism; D004798:Enzymes / Q000502:physiology*; D007700:Kinetics; D008956:Models, Chemical
D004798:Enzymes