A diffusion Michaelis-Menten mechanism: continuous conformational change in enzymatic kinetics.
We present a simple model which extends the Michaelis-Menten mechanism by incorporating a continuous protein conformational change in enzymatic catalysis. This model can represent a quantitative version for "rack" or "induced fit" mechanisms. In the steady-state it leads to an equation of the Michaelis-Menten form, but with the catalytic step at the active site showing strong dependence on solvent viscosity. We suggest that a careful examination of solvent viscosity effects on enzymatic activity may serve as a test for the conformational change hypothesis.
D001665:Binding Sites; D002384:Catalysis; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D012997:Solvents; D014783:Viscosity
D004798:Enzymes; D012997:Solvents