Mechanistic origin of the sigmoidal rate behaviour of glucokinase.

Model studies are presented which demonstrate that reactions proceeding by a random ternary-complex mechanism may exhibit most pronounced deviations from Michaelis-Menten kinetics even if the reaction is effectively ordered with respect to net reaction flow. In particular, the kinetic properties and reaction flow characteristics of glucokinase can be accounted for in such terms. It is concluded that insufficient evidence has been presented to support the idea that glucokinase operates by a 'mnemonical' type of mechanism involving glucose binding to distinct conformational states of free enzyme. The sigmoidal rate behaviour of glucokinase can presently be more simply explained in terms of glucose binding to differently ligated states of the enzyme.