Molecular and Cellular Biochemistry

, Volume 352, Issue 1, pp 87–89

Is the enzyme a powerful reactant of the biochemical reaction?


DOI: 10.1007/s11010-011-0742-4

Cite this article as:
Foigel, A.G. Mol Cell Biochem (2011) 352: 87. doi:10.1007/s11010-011-0742-4


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.


Enzymatic catalysisReaction mechanismα-ChymotrypsinMuscle contraction

Copyright information

© Springer Science+Business Media, LLC. 2011

Authors and Affiliations

  1. 1.Institute of Theoretical and Experimental Biophysics, Russian Ac. SciPushchinoRussia