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Biochemical characterization of recombinant dihydroorotate dehydrogenase from the opportunistic yeast Candida albicans

  • Elke Zameitat
  • Z. Gojkovic
  • W. Knecht
  • Jure Piskur
  • Monica Löffler
Publiceringsår: 2006
Språk: Engelska
Sidor: 3183-3191
Publikation/Tidskrift/Serie: The FEBS Journal
Volym: 273
Nummer: 14
Dokumenttyp: Artikel i tidskrift
Förlag: Federation of European Neuroscience Societies and Blackwell Publishing Ltd


Candida albicans is the most prevalent yeast pathogen in humans, and recently it has become increasingly resistant to the current antifungal agents. In this study we investigated C. albicans dihydroorotate dehydrogenase (DHODH, EC, which catalyzes the fourth step of de novo pyrimidine synthesis, as a new target for controlling infection. We propose that the enzyme is a member of the DHODH family 2, which comprises mitochondrially bound enzymes, with quinone as the direct electron acceptor and oxygen as the final electron acceptor. Full-length DHODH and N-terminally truncated DHODH, which lacks the targeting sequence and the transmembrane domain, were subcloned from C. albicans, recombinantly expressed in Escherichia coli, purified, and characterized for their kinetics and substrate specificity. An inhibitor screening with 28 selected compounds was performed. Only the dianisidine derivative, redoxal, and the biphenyl quinoline-carboxylic acid derivative, brequinar sodium, which are known to be potent inhibitors of mammalian DHODH, markedly reduced C. albicans DHODH activity. This study provides a background for the development of antipyrimidines with high efficacy for decreasing in situ pyrimidine nucleotide pools in C. albicans.


  • Biochemistry and Molecular Biology
  • DHODase
  • pathogenes
  • nucleic acid precursors
  • yeast


  • ISSN: 1742-464X

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