title: Is the enzyme a powerful reactant of the biochemical reaction?
abstract: The mainstream explanation of enzyme catalysis relies on the assumption that enzymes can utilize the binding energy. The author suggest that (i) an enzyme with excess free energy first gives a group from its active site into the final place of the bound reactant (substrate) in order to break the first initial chemical bond; (ii) this enzyme accepts a similar group from the second bound reactant (or second group in the case of the single-substrate) into active site and finish the substrate conversion and enzyme regeneration. The detailed mechanisms of the well-studied reactions of peptide bond hydrolysis catalyzed by α-chymotrypsin and the glyceraldehyde-3-phosphate interconversion steps in glycolysis are in accordance with the proposed theoretical conclusions.
authors.affiliation: Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia. agfoigel@rambler.ru
authors.forename: Alexander G
authors.initials: AG
authors.lastname: Foigel
mesh_terms: D020134:Catalytic Domain; D004798:Enzymes / Q000378:metabolism*; D008962:Models, Theoretical
chemical_list: D004798:Enzymes