Journal
FEBS LETTERS
Volume 529, Issue 2-3, Pages 346-350Publisher
WILEY
DOI: 10.1016/S0014-5793(02)03425-7
Keywords
dihydroorotate dehydrogenase; pyrimidines; quinones; recombinant; Arabidopsis thaliana
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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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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