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Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri

Zameitat, Elke; Knecht, W.; Piskur, Jure LU and Löffler, M. (2004) In FEBS Letters 568(1-3). p.129-134
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.... (More)
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 (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Dihydroorotate dehydrogenase, Schizosaccharomyces pombe, Saccharomyces kluyveri, Saccharomyces cerevisiae, nucleic acid precursor, evolution, yeast, enzyme, Protein expression, Inhibition
in
FEBS Letters
volume
568
issue
1-3
pages
129 - 134
publisher
Wiley-Blackwell
external identifiers
  • wos:000222205200025
  • scopus:2942529243
ISSN
1873-3468
DOI
10.1016/j.febslet.2004.05.017
language
English
LU publication?
yes
id
fc9c5e14-6d1a-4104-8f9a-0d10d1f542b4 (old id 740292)
date added to LUP
2008-01-09 15:17:51
date last changed
2017-10-29 04:10:35
@article{fc9c5e14-6d1a-4104-8f9a-0d10d1f542b4,
  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},
  author       = {Zameitat, Elke and Knecht, W. and Piskur, Jure and Löffler, M.},
  issn         = {1873-3468},
  keyword      = {Dihydroorotate dehydrogenase,Schizosaccharomyces pombe,Saccharomyces kluyveri,Saccharomyces cerevisiae,nucleic acid precursor,evolution,yeast,enzyme,Protein expression,Inhibition},
  language     = {eng},
  number       = {1-3},
  pages        = {129--134},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri},
  url          = {http://dx.doi.org/10.1016/j.febslet.2004.05.017},
  volume       = {568},
  year         = {2004},
}