Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes
Authors:
- Alexandra UllrichAUAlexandra Ullrich
- Wolfgang KnechtWKWolfgang Knecht
- Monika LöfflerMLMonika Löffler
- 18 September 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 529 (2-3) , 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.Keywords
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