Proteins pp 615-622 | Cite as

Imidoesters and the Mechanism of Liver Alcohol Dehydrogenase

  • Bryce V. Plapp
Chapter

Abstract

Protein chemists have just begun to exploit the full potential of imidoesters, which react specifically with amino groups (1,2), for studying protein structure and function. In this article, the uses of imidoesters to investigate the role of a lysine residue at the active site of liver alcohol dehydrogenase and to prepare derivatives for other mechanistic studies are illustrated. Furthermore, the kinetics of reactions of ethyl acetimidate and the optimal conditions for protein modification are discussed. The results presented here also support several theses of protein chemistry, which can apply to other types of chemical modification.

Keywords

Alcohol Dehydrogenase Diethyl Pyrocarbonate Imidazole Group Zinc Hydroxide Coenzyme Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Hunter, M. J., and Ludwig, M. L. (1972) Methods Enzymol. 25, 585–596.CrossRefGoogle Scholar
  2. 2.
    Inman, J. K., Perham, R. N., DuBois, G. C., and Appela, E. (1983) Methods Enzymol. 91, 559–569.PubMedCrossRefGoogle Scholar
  3. 3.
    Benisek, W. F., and Richards, F. M. (1968) J. Biol. Chem. 243, 4267–4271.PubMedGoogle Scholar
  4. 4.
    Plapp, B. V., Moore, S., and Stein, W. H. (1971) J. Biol. Chem. 246, 939–945.PubMedGoogle Scholar
  5. 5.
    Plapp, B. V. (1970) J. Biol. Chem. 245, 1727–1735.PubMedGoogle Scholar
  6. 6.
    Sogin, D. C., and Plapp, B. V. (1975) J. Biol. Chem. 250, 205–210.PubMedGoogle Scholar
  7. 7.
    Dworschack, R. T., Tarr, G., and Plapp, B. V. (1975) Biochemistry 14, 200–203.PubMedCrossRefGoogle Scholar
  8. 8.
    Zoltobrocki, M., Kim, J. C., and Plapp, B. V. (1974) Biochemistry 13, 899–903.PubMedCrossRefGoogle Scholar
  9. 9.
    Fries, R. F., Bohlken, D. P., Blakley, R. T., and Plapp, B. V. (1975) Biochemistry 14, 5233–5238.PubMedCrossRefGoogle Scholar
  10. 10.
    Plapp, B. V., Brooks, R. L., and Shore, J. D. (1973) J. Biol. Chem. 248, 3470–3475.PubMedGoogle Scholar
  11. 11.
    Dworschack, R. T., and Plapp, B. V. (1977) Biochemistry 16, 2716–2725.PubMedCrossRefGoogle Scholar
  12. 12.
    Eklund, H., Samama, J.-P., Wallen, L., Branden, C.–I., Akeson, A, and Jones, T. A. (1981) J. Mol. Biol. 146, 561–587.PubMedCrossRefGoogle Scholar
  13. 13.
    Plapp, B. V., Eklund, H., Jones, T. A., and Branden, C.-I. (1983) J. Biol. Chem. 258, 5537–5547.PubMedGoogle Scholar
  14. 14.
    Plapp, B. V., Sogin, D. C., Dworschack, R. T., Bohlken, D. P., Woenckhaus, C., and Jeck, R., manuscript in preparation.Google Scholar
  15. 15.
    Parker, D. M., Hardman, M. J., Plapp, B. V., Holbrook, J. J., and Shore, J. D. (1978) Biochem. J. 173, 269–275.PubMedGoogle Scholar
  16. 16.
    Browne, D. T., and Kent, S. B. H. (1975) Biochem. Biophys. Res. Commun. 67, 126–132, 133–138.PubMedCrossRefGoogle Scholar
  17. 17.
    Hennecke, M., and Plapp, B.V., manuscript in preparation.Google Scholar
  18. 18.
    Eklund, H., Plapp, B. V., Samama, J.-P., and Branden, C.-I. (1982) J. Biol. Chem. 257, 14349–14358.PubMedGoogle Scholar
  19. 19.
    Kvassman, J., and Pettersson, G. (1978) Eur. J. Biochem. 87, 417–427.PubMedCrossRefGoogle Scholar
  20. 20.
    Hennecke, M., and Plapp, B. V. (1983) Biochemistry 22, 3721–3728.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Bryce V. Plapp
    • 1
  1. 1.Department of BiochemistryThe University of IowaIowa CityUSA

Personalised recommendations