A comprehensive theory for relating free-energy profiles to kinetic equations of enzyme reactions has been developed. It enables expression of the overall rate and the concentrations of reaction intermediates in terms of the heights of peaks in free-energy profiles for various reactions. The reactions include consecutive reactions with intermittent irreversible steps, those with dead-end side r...

Enzyme kinetics are usually described by the Michaelis-Menten equation, where the time-dependent decrease of substrate (-dS/dt) is a hyperbolic function of maximal velocity (Vmax), Michaelis constant (Km), and amount of substrate (S). Because the Michaelis-Menten function in its most general meaning requires an assumption of steady-state, it is less curvilinear than true enzyme kinetics. A satu...

1. A theory is developed to account for the kinetics of coupled-enzyme reactions without assuming that the second reaction follows first-order kinetics. 2. A simple procedure is described for applying the theory to the practical design ofenzyme assays. 3. The validity of the theory is confirmed for the assay of glucokinase with glucose 6-phosphate dehydrogenase as coupling enzyme. 4. The possib...

A limited number of publicly available resources provide access to enzyme kinetic parameters. These have been compiled through manual data mining of published papers, not from the original, raw experimental data from which the parameters were calculated. This is largely due to the lack of software or standards to support the capture, analysis, storage and dissemination of such experimental data...