Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/db27e89d-6542-4034-8b54-a99e1d7c6024
- author
- Ullrich, Alexandra ; Knecht, Wolfgang LU ; Piskur, Jure LU and Löffler, Monika
- publishing date
- 2002-10-09
- 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}}, }