Journal article
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.
| Language: | English |
|---|---|
| Year: | 2002 |
| Pages: | 346-350 |
| ISSN: | 18733468 and 00145793 |
| Types: | Journal article |
| DOI: | 10.1016/s0014-5793(02)03425-7 |
Amino Acid Sequence Arabidopsis Base Sequence DNA Primers DNA, Complementary Dihydroorotate Dehydrogenase Electrophoresis, Polyacrylamide Gel Humans Kinetics Molecular Sequence Data Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Recombinant Proteins Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Substrate Specificity
