title: Energetics of enzyme catalysis. I. Isotopic experiments, enzyme interconversion, and oversaturation.
abstract: An enzyme-catalyzed interconversion of one substrate, S, and one product P, by an enzyme that exists in two forms E1 and E2 where E1 binds S and E2 binds P, is considered S + E1 in equilibrium E1S in equilibrium E2P in equilibrium E2 + P. Under reversible conditions (where the concentrations of S and P are not far removed from their equilibrium values) it is shown that, in addition to the usual unsaturated and saturated behaviour there exists a third regime at high substrate concentration: the oversaturated region. In this region, the rate-limiting transition state is the interconversion of the unliganded forms of the enzyme: E1 and E2. Expressions for six different experiments involving deuterium, tritium and 14C labels are presented. By considering the results from these experiments, the nature and importance of the enzyme interconversion steps can be elucidated.
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; D003903:Deuterium; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D013816:Thermodynamics; D014316:Tritium
chemical_list: D004798:Enzymes; D014316:Tritium; D003903:Deuterium