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.
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Acknowledgments
The author thank Prof. E. I. Maevsky of the Institute of Theoretical and Experimental Biophysics for his remarks on this article. The author would also like to thank Mr. Ilia Stambler of Bar-Ilan University for the manuscript editing.
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Foigel, A.G. Is the enzyme a powerful reactant of the biochemical reaction?. Mol Cell Biochem 352, 87–89 (2011). https://doi.org/10.1007/s11010-011-0742-4
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DOI: https://doi.org/10.1007/s11010-011-0742-4