Molecular and Cellular Biochemistry

, Volume 352, Issue 1–2, pp 87–89 | Cite as

Is the enzyme a powerful reactant of the biochemical reaction?

Article
  • 89 Downloads

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.

Keywords

Enzymatic catalysis Reaction mechanism α-Chymotrypsin Muscle contraction 

Notes

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.

References

  1. 1.
    Fischer E (1894) Einfluss der configuration auf die wirkung der enzyme. Ber Dtsch Chem Ges 27:2985–2993. doi: 10.1002/cber.18940270364 CrossRefGoogle Scholar
  2. 2.
    Haldane JBS (1930) Enzymes. Green and Co, LondonGoogle Scholar
  3. 3.
    Koshland DE, Neet KE (1968) The catalytic and regulatory properties of enzymes. Annu Rev Biochem 37:359–410PubMedCrossRefGoogle Scholar
  4. 4.
    Wolfenden R, Snider MJ (2001) The depth of chemical time and the power of enzymes as catalysts. Acc Chem Res 34:938–945PubMedCrossRefGoogle Scholar
  5. 5.
    Wolfenden R (2003) Thermodynamic and extrathermodynamic requirements of enzyme catalysis. Biophys Chem 105:559–572PubMedCrossRefGoogle Scholar
  6. 6.
    Fogel AG (1982) Cooperativity of enzymatic reactions and molecular aspects of energy transduction. Mol Cell Biochem 47:59–64PubMedCrossRefGoogle Scholar
  7. 7.
    Hengge AC, Stein RL (2004) Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates. Biochemistry 43:742–747PubMedCrossRefGoogle Scholar
  8. 8.
    Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D (1991) Structure of the triosephosphate isomerase-phosphoglucolohydroxamate complex: an analogue of the intermediate on the reaction pathway. Biochemistry 30:5821–5826PubMedCrossRefGoogle Scholar
  9. 9.
    Bash PA, Field MJ, Davenport RC, Petsko GA, Ringe D, Karplus M (1991) Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry 30:5826–5832PubMedCrossRefGoogle Scholar
  10. 10.
    Jedrzejas MJ (2000) Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Prog Biophys Mol Biol 73:263–287PubMedCrossRefGoogle Scholar
  11. 11.
    Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10:4617–4624PubMedCrossRefGoogle Scholar
  12. 12.
    Holmes KC, Angert I, Kull FJ, Jahn W, Schröder RR (2003) Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425:423–427PubMedCrossRefGoogle Scholar
  13. 13.
    Siemankowski RF, Wiseman MO, White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82:658–662PubMedCrossRefGoogle Scholar
  14. 14.
    White HD, Belknap B, Webb MR (1997) Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry 36:11828–11836PubMedCrossRefGoogle Scholar
  15. 15.
    Tirosh R, Low WZ, Oplatka A (1990) Translational motion of actin filaments in the presence of heavy meromyosin and MgATP as measured by Doppler broadening of laser light scattering. Biochim Biophys Acta 1037:274–280PubMedCrossRefGoogle Scholar
  16. 16.
    Tirosh R (2006) Ballistic protons and microwave-induced water solutions in bioenergetic transformations. Int J Mol Sci 7:320–345CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC. 2011

Authors and Affiliations

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

Personalised recommendations