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Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes

Ullrich, Alexandra ; Knecht, Wolfgang LU ; Piskur, Jure LU and Löffler, Monika (2002) In FEBS Letters 529(2-3). p.346-350
Abstract

The mitochondrial membrane bound dihydroorotate dehydrogenase (DHODH; EC 1.3.99.11) catalyzes the fourth step of pyrimidine biosynthesis. By the present correction of a known cDNA sequence for Arabidopsis thaliana DHODH we revealed the importance of the very C-terminal part for its catalytic activity and the reason why--in contrast to mammalian and insect species--the recombinant plant flavoenzyme was unaccessible to date for in vitro characterization. Structure-activity relationship studies explained that potent inhibitors of animal DHODH do not significantly affect the plant enzyme. These difference could be exploited for a novel approach to herb or pest growth control by limitation of pyrimidine nucleotide pools.

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author
; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Amino Acid Sequence, Arabidopsis/enzymology, Base Sequence, DNA Primers, DNA, Complementary, Electrophoresis, Polyacrylamide Gel, Humans, Kinetics, Molecular Sequence Data, Oxidoreductases/antagonists & inhibitors, Oxidoreductases Acting on CH-CH Group Donors, Recombinant Proteins/antagonists & inhibitors, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Substrate Specificity
in
FEBS Letters
volume
529
issue
2-3
pages
346 - 350
publisher
Wiley-Blackwell
external identifiers
  • scopus:0037048657
  • pmid:12372626
ISSN
0014-5793
DOI
10.1016/s0014-5793(02)03425-7
language
English
LU publication?
no
id
db27e89d-6542-4034-8b54-a99e1d7c6024
date added to LUP
2020-07-22 14:22:37
date last changed
2024-04-03 11:38:43
@article{db27e89d-6542-4034-8b54-a99e1d7c6024,
  abstract     = {{<p>The mitochondrial membrane bound dihydroorotate dehydrogenase (DHODH; EC 1.3.99.11) catalyzes the fourth step of pyrimidine biosynthesis. By the present correction of a known cDNA sequence for Arabidopsis thaliana DHODH we revealed the importance of the very C-terminal part for its catalytic activity and the reason why--in contrast to mammalian and insect species--the recombinant plant flavoenzyme was unaccessible to date for in vitro characterization. Structure-activity relationship studies explained that potent inhibitors of animal DHODH do not significantly affect the plant enzyme. These difference could be exploited for a novel approach to herb or pest growth control by limitation of pyrimidine nucleotide pools.</p>}},
  author       = {{Ullrich, Alexandra and Knecht, Wolfgang and Piskur, Jure and Löffler, Monika}},
  issn         = {{0014-5793}},
  keywords     = {{Amino Acid Sequence; Arabidopsis/enzymology; Base Sequence; DNA Primers; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Humans; Kinetics; Molecular Sequence Data; Oxidoreductases/antagonists & inhibitors; Oxidoreductases Acting on CH-CH Group Donors; Recombinant Proteins/antagonists & inhibitors; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Substrate Specificity}},
  language     = {{eng}},
  month        = {{10}},
  number       = {{2-3}},
  pages        = {{346--350}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes}},
  url          = {{http://dx.doi.org/10.1016/s0014-5793(02)03425-7}},
  doi          = {{10.1016/s0014-5793(02)03425-7}},
  volume       = {{529}},
  year         = {{2002}},
}