title: A view at the millennium: the efficiency of enzymatic catalysis.
abstract: Binding TS in preference to S and increasing TDeltaS++by freezing out motions in E X S and E X TS have been accepted as the driving forces in enzymatic catalysis; however, the smaller value of DeltaG++ for a one-substrate enzymatic reaction, as compared to its nonenzymatic counterpart, is generally the result of a smaller value of DeltaH++. Ground-state conformers (E X NACs) are formed in enzymatic reactions that structurally resemble E X TS. E X NACs are in thermal equilibrium with all other E X S conformers and are turnstiles through which substrate molecules must pass to arrive at the lowest-energy TS. TS in E X TS may or may not be bound tighter than NAC in E X NAC.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Bruice
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D019277:Entropy; D004798:Enzymes / Q000737:chemistry*; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D004798:Enzymes