NMR in the Study of Enzyme Catalysis

  • H. Rüterjans
Conference paper
Part of the Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden book series (MOSBACH, volume 32)

Abstract

In order to understand enzyme catalysis it is necessary to know the specific spatial arrangement of the active site amino acid side chains. By interaction with each other or with a coenzyme the functional groups of the active site form a sort of polar complex which enables the formation of the transition state of the enzyme substrate complex. However, because of the flexibility of the protein structure, equilibria of these manifold interactions have to be considered. If a distinct interaction between two side chains is needed for the catalytic activity, only the enzyme species with this interaction is active, whereas all other species should be inactive.

Keywords

Crystallization Manifold Catalysis Carboxylate Phenyl 

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References

  1. 1.
    Dwek RA (1973) Nuclear magnetic resonance in biochemistry, application to enzyme systems. Claredon Press, OxfordGoogle Scholar
  2. 2.
    Blomberg F, Maurer W, Rüterjans H (1977) J Am Chem Soc 99: 8149PubMedCrossRefGoogle Scholar
  3. 3.
    Bachovchin WW, Roberts JD (1978) J Am Chem Soc 100: 8041CrossRefGoogle Scholar
  4. 4.
    Blow DM, Steitz TA, (1970): Ann Rev. Biochem 39: 63PubMedCrossRefGoogle Scholar
  5. 5.
    Rüterjans H, Witzel H (1969) Eur J Biochem 9: 118PubMedCrossRefGoogle Scholar
  6. 6.
    Haar W, Thompson JC, Maurer W, Rüterjans H (1973) Eur J Biochem 40: 259PubMedCrossRefGoogle Scholar
  7. 7.
    Haar W, Maurer W, Rüterjans H (1974) Eur J Biochem 44: 201PubMedCrossRefGoogle Scholar
  8. 8.
    Richards FM, Wyckoff HW (1971) In: Boyer BD (ed) The enzymes, vol IV. Academic Press, London New York, p 647Google Scholar
  9. 9.
    Büchner P, Blomberg F, Rüterjans H (1978) In: Pallman B (ed) Nuclear magnetic resonance spectroscopy in molecular biology. D Reidel Publ Comp, Dordrecht, Holland, p 53CrossRefGoogle Scholar
  10. 10.
    Wyman J (1964) Adv Protein Chem 19: 224Google Scholar
  11. 11.
    Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 89PubMedCrossRefGoogle Scholar
  12. 12.
    Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 79PubMedCrossRefGoogle Scholar
  13. 13.
    Steigemann W, Weber E (1979) J Mol Biol 127: 309; Huber R, Epp O, Steigemann W, Formanek H (1971) Eur J Biochem 19: 32Google Scholar
  14. 14.
    Krümpelmann D, Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 103PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1981

Authors and Affiliations

  • H. Rüterjans
    • 1
  1. 1.Institut für Biophysikalische Chemie der Johann Wolfgang Goethe-UniversitätFrankfurtGermany

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