title: Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviour.
abstract: Most enzymes react in vivo under reversible conditions where the substrate and product concentrations are not far removed from equilibrium values. Under these conditions when the concentration of substrate is increased, in addition to the usual unsaturated and saturated behaviour we find a third type of kinetic regime at high substrate concentration-oversaturation. In this regime the rate limiting transition state involves interconversion of free enzyme forms. For a one substrate/one product enzyme, case diagrams can be constructed which depict the kinetic behaviour as a function of substrate and product concentrations. Six different cases are found and are discussed with the relevant free energy profiles. A systematic procedure is described for the investigation and construction of the case diagram.
authors: Department of Chemistry, Imperial College, London, U.K.
authors: W J
authors: WJ
authors: Albery
authors: J R
authors: JR
authors: Knowles
mesh_terms: D002384:Catalysis; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D013816:Thermodynamics
chemical_list: D004798:Enzymes