Journal of Protein Chemistry

, Volume 13, Issue 7, pp 619–627

Purification and characterization of fungal and mammalian phosphomannose isomerases

  • Amanda E. I. Proudfoot
  • Mark A. Payton
  • Timothy N. C. Wells

DOI: 10.1007/BF01890460

Cite this article as:
Proudfoot, A.E.I., Payton, M.A. & Wells, T.N.C. J Protein Chem (1994) 13: 619. doi:10.1007/BF01890460


Phosphomannose isomerase (PMI) is essential for the production of yeast cell walls. An inhibitor which inhibits the fungal enzyme without altering the activity of the mammalian enzyme would be a potential fungicidal agent, increasingly important in view of the increasing mortality from visceral mycoses in immunosuppressed patients. We have purified human, porcine, andCandida albicans enzymes 29,000-fold to homogeneity, and characterized their physical properties, as well as their kinetic parameters, inhibition constants, andpH dependences. Surprisingly, in view of the large differences betweenPseudomonas aerugenosa andSaccharomyces cerevisiae PMI, the human andC. albicans enzymes are almost identical. We suggest therefore that species-selective inhibition of the fungal rather than mammalian enzyme may require molecules which bind away from the substrate binding pocket of the enzyme.

Key words

Phosphomannose isomeraseCandida albicanshumanporcinepurificationcharacterization



phosphomannose isomerase




4-(2-hydroxyethyl)-piperazine-1-ethanesulfonic acid


2-(N-morphilino) ethanesulfonic acid

Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Amanda E. I. Proudfoot
    • 1
  • Mark A. Payton
    • 1
  • Timothy N. C. Wells
    • 1
  1. 1.Glaxo Institute for Molecular BiologyGenevaSwitzerland