Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri

Research output: Contribution to journalArticle

Abstract

Genes for two structurally and functionally different dihydroorotate dehydrogenases (DHODHs, EC 1.3.99.11), catalyzing the fourth step of pyrimidine biosynthesis, have been previously found in yeast Saccharomyces kluyveri. One is closely related to the Schizosaccharomyces pombe mitochondrial family 2 enzymes, which use quinones as direct and oxygen as the final electron acceptor. The other one resembles the Saccharomyces cerevisiae cytosolic family 1A fumarate-utilizing DHODH. The DHODHs from S. kluyveri, Sch. pombe and S. cerevisiae, were expressed in Escherichia coli and compared for their biochemical properties and interaction with inhibitors. Benzoates as pyrimidine ring analogs were shown to be selective inhibitors of cytosolic DHODs. This unique property of Saccharomyces DHODHs could appoint DHODH as a species-specific target for novel anti-fungal therapeutics

Details

Authors
  • Elke Zameitat
  • W. Knecht
  • Jure Piskur
  • M. Löffler
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • Dihydroorotate dehydrogenase, Schizosaccharomyces pombe, Saccharomyces kluyveri, Saccharomyces cerevisiae, nucleic acid precursor, evolution, yeast, enzyme, Protein expression, Inhibition
Original languageEnglish
Pages (from-to)129-134
JournalFEBS Letters
Volume568
Issue number1-3
Publication statusPublished - 2004
Publication categoryResearch
Peer-reviewedYes