Is the enzyme a powerful reactant of the biochemical reaction?

@article{Foigel2011IsTE,
  title={Is the enzyme a powerful reactant of the biochemical reaction?},
  author={A. G. Foigel},
  journal={Molecular and Cellular Biochemistry},
  year={2011},
  volume={352},
  pages={87-89}
}
  • A. G. Foigel
  • Published 2011
  • Chemistry, Medicine
  • Molecular and Cellular Biochemistry
  • 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… CONTINUE READING
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    References

    SHOWING 1-10 OF 14 REFERENCES
    The depth of chemical time and the power of enzymes as catalysts.
    • 600
    • PDF
    Thermodynamic and extrathermodynamic requirements of enzyme catalysis.
    • 71
    • PDF
    Computer simulation and analysis of the reaction pathway of triosephosphate isomerase.
    • 194
    Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates.
    • 18
    Mechanism of adenosine triphosphate hydrolysis by actomyosin.
    • 1,125
    • PDF
    Cooperativity of enzymatic reactions and molecular aspects of energy transduction
    • A. Fogel
    • Chemistry, Medicine
    • Molecular and Cellular Biochemistry
    • 2004
    • 2
    ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle.
    • 359
    • PDF
    Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • 349
    Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase.
    • M. Jedrzejas
    • Biology, Medicine
    • Progress in biophysics and molecular biology
    • 2000
    • 121
    • PDF