Skip to main content
SpringerLink
Log in

Determination of the pKa for histidine-51 residue in the ternary complex of horse liver alcohol dehydrogenase

  • Original Articles
  • Published:
Archives of Pharmacal Research Aims and scope Submit manuscript

Abstract

The pKa value of histidine-51 residue was determined by the pH dependency of contents of NADH bound to the active site in the horse liver alcohol dehydrogenase and % inactivation with diethyl pyrocarbonate treatment of the enzyme. The pKa for His-51 was ∼7.15 in the ternary complex and ∼6.7 in the enzyme itself.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Literature Cited

  1. Eklund, H., Plapp, B. V., Samama, J.-P. and Bränden, C.-I.: Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.J. Biol. Chem. 257, 1434 (1982).

    Google Scholar 

  2. Kvassman, J. and Petterson, G.: Unified mechanism for proton-transfer reactions affecting the catalytic activity of liver alcohol dehydrogenase,Eur. J. Biochem. 103, 565 (1980).

    Article  PubMed  CAS  Google Scholar 

  3. Kvassman, J. and Petterson, G.: Effect of pH on the process of ternary complex interconversion in the liver alcohol dehydrogenase reaction.Eur. J. Biochem. 87, 417 (1978).

    Article  PubMed  CAS  Google Scholar 

  4. Brooks, R. L., Shore, J. D. and Gutfreund, H.: The effects of pH and temperature on hydrogen transfer in the liver alcohol dehydrogenase mechanism.J. Biol. Chem. 247, 2382 (1972).

    PubMed  CAS  Google Scholar 

  5. Sekhar, V. C. and Plapp, B. V.: Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide.Biochemistry 27, 5082 (1988).

    Article  PubMed  CAS  Google Scholar 

  6. Kvassman, J. and Pettersson, G.: Effect of pH on coenzyme binding to liver alcohol dehydrogenase.Eur. J. Biochem. 100, 115 (1979).

    Article  PubMed  CAS  Google Scholar 

  7. Shore, J. D., Gutfreund, H., Brooks, R. L., Santiago, D. and Santiago, P.: Proton equilibria and kinetics in the liver alcohol dehydrogenase reaction mechanism.Biochemistry. 13, 4185 (1974).

    Article  PubMed  CAS  Google Scholar 

  8. Hennecke, M. and Plapp, B. V.: Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase.Biochemistry. 22, 3721 (1983).

    Article  PubMed  CAS  Google Scholar 

  9. Bonnichsen, R. K.: Crystalline animal alcohol dehydragenase.Acta. Chem. Scand. 4, 715 (1950).

    Article  CAS  Google Scholar 

  10. Wratten, C. C. and Cleland, W. W.: Product inhibition studies on yeast and liver alcohol dehydrogenase.Biochemistry.2, 935 (1963).

    Article  PubMed  CAS  Google Scholar 

  11. Miles, E. W.: Modification of histidine residue in proteins by diethyl pyrocarbonate.Methods in Enzymol. 47, 431 (1977).

    Article  CAS  Google Scholar 

  12. Melchior, W. B. and Fahrney, D.: Ethoxyformylation of proteins: Reaction of ethoxyformic anhydride with chymotrypsin, pepsin and pancreatic ribonuclease at pH 4.Biochemistry. 9, 251 (1970).

    Article  PubMed  CAS  Google Scholar 

  13. Dworschack, R. T. and Plapp, B. V.: Kinetics of native and activated isozyme of horse liver alcohol dehydrogenase.Biochemistry,16, 111 (1977).

    Article  PubMed  CAS  Google Scholar 

  14. Dworschack, R. T. and Plapp, B. V.: pH isotope and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenase.Biochemistry,16, 2716 (1977).

    Article  PubMed  CAS  Google Scholar 

  15. Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B. O., Tapia, O., Bränden, C.-I. and Åkeson, Å.: Three-dimentional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution.J. Mol. Biol. 102, 27 (1976).

    Article  PubMed  CAS  Google Scholar 

  16. Eklund, H. and Branden, C.-I.:in Active sites of enzymes (Jurnak, F. A. and McPherson, A., Eds) pp. 73–142, Wiley, New York (1987).

    Google Scholar 

  17. Sartorius, C., Gerber, M., Zeppezauer, M. and Dunn, M. F.: Active-site Cobalt(II)-substituted horse liver alcohol dehydrogenase: Characterization of intermediates in the oxidation and reduction processes as a function of pH.Biochemistry.26, 871 (1987).

    Article  PubMed  CAS  Google Scholar 

  18. Morris, D. L. and Mckinley-Mckee, J. S.: The histidines in liver alcohol dehydrogenase-chemical modification with diethyl pyrocarbonate.Eur. J. Biochem. 29, 515 (1972).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. College of Pharmacy, Ewha Womans University, 120-750, Seoul, Korea

    Kang Man Lee & Su Yeon Son

Authors
  1. Kang Man Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Su Yeon Son
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lee, K.M., Son, S.Y. Determination of the pKa for histidine-51 residue in the ternary complex of horse liver alcohol dehydrogenase. Arch. Pharm. Res. 15, 229–233 (1992). https://doi.org/10.1007/BF02974060

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02974060

Keywords

Search

Navigation