Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri
Author
Summary, in English
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
Publishing year
2004
Language
English
Pages
129-134
Publication/Series
FEBS Letters
Volume
568
Issue
1-3
Document type
Journal article
Publisher
Wiley-Blackwell
Topic
- Biological Sciences
Keywords
- Dihydroorotate dehydrogenase
- Schizosaccharomyces pombe
- Saccharomyces kluyveri
- Saccharomyces cerevisiae
- nucleic acid precursor
- evolution
- yeast
- enzyme
- Protein expression
- Inhibition
Status
Published
ISBN/ISSN/Other
- ISSN: 1873-3468