title: Transition state variation in enzymatic reactions.
abstract: Experimental analysis of enzymatic transition states by kinetic isotope effect methods has established geometric variation in related transition state structures. Differences are apparent in development of the reaction coordinate, in solvolytic transition states relative to those in enzymatic catalytic sites, in the stereochemistry of related substrates at the transition state, and in reactions catalyzed by related enzymes.
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. vern@aecom.yu.edu
authors.forename: V L
authors.initials: VL
authors.lastname: Schramm
mesh_terms: D002384:Catalysis; D045647:DNA Glycosylases; D004798:Enzymes / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D009699:N-Glycosyl Hydrolases / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry
chemical_list: D004798:Enzymes; D011506:Proteins; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases