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

@article{Ullrich2002PlantDD,
  title={Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes.},
  author={Alexandra Ullrich and Wolfgang Knecht and Jure Pi{\vs}kur and Monika L{\"o}ffler},
  journal={FEBS letters},
  year={2002},
  volume={529 2-3},
  pages={346-50}
}
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… CONTINUE READING