Biochemical Characterization of Dihydrofolate Reductase of Halobacterium Volcanii

  • Tal Zusman
  • Moshe Mevarech
Part of the NATO ASI Series book series (NSSA, volume 201)


The enzymatic activity of the enzyme dihydrofolate reductase of Halobacterium volcanii depends on salt concentration. the following communication describes the effect of salt concentration and pH on the catalytic parameters of this enzyme. In addition, the mode of inhibition of three different inhibitors of DHFR was studied.


Salt Concentration High Salt Concentration Dihydrofolate Reductase Halophilic Bacterium Hydride Transfer 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. [1]
    D. J. Kushner, The Halobacteriaceae, in “The Bacteria”, Vol. 8, pp. 171–214, C. R. Woese and R. S. Wolfe, eds, Academic Press, New York (1985)Google Scholar
  2. [2]
    J. H. B. Christian and J. A. Waltho, Solute concentration within cells of halophilic and non-halophilic bacteria, Biochitn. Biophys. Acta65: 506 (1962)CrossRefGoogle Scholar
  3. [3]
    J. K. Lanyi, Salt dependent properties of proteins from extremely halophilic bacteria, Bacteriol. Rev.38: 272 (1974)PubMedGoogle Scholar
  4. [4]
    R. Reistad, On the composition and nature of the bulk protein of extremely halophilic bacteria, Arch. Microbiol.71: 353 (1970)Google Scholar
  5. [5]
    G. Zaccai, G. J. Bunick and H. Eisenberg, Denaturation of a halophilic enzyme monitored by small-angle neutron scattering, J. Mol. Biol.192: 155 (1986)PubMedCrossRefGoogle Scholar
  6. [6]
    R. L. Blakley, Chemistry and biochemistry of folates, in “Folates and Pteridines”, Vol. 1, pp. 191–253, R. L. Blakley and S. J. Benkovic, eds. Wiley & Sons, New York (1984)Google Scholar
  7. [7]
    J. J. Burchall and G. H. Hitchings, Inhibitor binding analysis of dihydrofolate reductases from various species, Mol. Pharmacol.1: 126 (1965)PubMedGoogle Scholar
  8. [8]
    T. Zusman, I. Rosenshine, G. Boehm, R. Jaenicke, B. Leskiw and M. Mevarech, Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii, J. Biol. Chem.264: 18878 (1989)PubMedGoogle Scholar
  9. [9]
    I. Rosenshine, T. Zusman, R. Werczberger and M. Mevarech, Amplification of specific DNA sequences correlates with resistance of the archaebacterium Halobacterium volcaniito dihydrofolate reductase inhibitors trimethoprim and methotrexate, Mol. Gen. Genet.208: 518 (1987)CrossRefGoogle Scholar
  10. [10]
    B. L. Hiilcoat, P. F. Nixon and R. L. Blakey, Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase, Anal. Biochem.21: 178 (1967)CrossRefGoogle Scholar
  11. [11]
    C. A. Fierke, K. A. Johnson and S. J. Benkovic, Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli, Biochemistry 26: 4085 (1987)PubMedCrossRefGoogle Scholar
  12. [12]
    A. J. Russel and A. R. Fersht, Rational modification of enzyme catalysis by engineering surface charge, Nature328: 496 (1987)CrossRefGoogle Scholar
  13. [13]
    K. M. Perry, J. J. Onuffer, N. A. Touchette, C. S. Hendon, M. S. Gittelman, C. R. Mathews, J. T. Chen, R. J. Mayer, K. Taira, S. J. Benkovic, E. E. Howell and J. Kraut, Effect of single amino acid replacements on the folding and stability of dihydrofolate from Escherichia coli, Biochemistry26: 2674 (1987)PubMedCrossRefGoogle Scholar
  14. [14]
    S. R. Stone and J. F. Morrison, Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli, Biochemistry21: 3757 (1982)PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Tal Zusman
    • 1
  • Moshe Mevarech
    • 1
  1. 1.Department of Microbiology George S. Wise Faculty of Life SciencesTel Aviv UniversityTel AvivIsrael

Personalised recommendations