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Ullrich, A. et al.

Ullrich, Knecht, Piskur, Löffler,

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

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.[1]

References

Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes. Ullrich, A., Knecht, W., Piskur, J., Löffler, M. FEBS Lett. (2002) [Pubmed]

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