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Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes
Author(s) -
Ullrich Alexandra,
Knecht Wolfgang,
Piskur Jure,
Löffler Monika
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03425-7
Subject(s) - dihydroorotate dehydrogenase , biochemistry , pyrimidine metabolism , enzyme , arabidopsis thaliana , biology , pyrimidine , dehydrogenase , complementary dna , gene , purine , mutant
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.