EC Number |
General Information |
Reference |
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1.3.5.2 | metabolism |
DHODH is the fourth enzyme in the biosynthesis of pyrimidines |
713150 |
1.3.5.2 | physiological function |
DHODH catalyzes the rate-limiting step in the pyrimidine biosynthetic pathway |
712475 |
1.3.5.2 | physiological function |
dihydroorotate dehydrogenase is associated with mitochondrial electron transport and required for de novo pyrimidine synthesis, and is required for N-(4-hydroxyphenyl)retinamide-induced reactive oxygen species production and apoptosis. Chemical inhibition of DHODH activity or the reduction of DHODH protein suppresses 4HPR-induced ROS production and apoptosis in transformed skin and prostate epithelial cells, overview |
712071 |
1.3.5.2 | physiological function |
enzyme employs a two-site Ping-Pong steady-state mechanism of catalysis. In the first and reductive half-reaction, the enzyme oxidizes dihydroorotate to orotate with the concomitant reduction of FMN to FMNH2. In the second and oxidative half-reaction, FMNH2 is reoxidized by reducing the quinone to quinol |
762769 |
1.3.5.2 | physiological function |
Plasmodium DHODH is an essential mitochondrial enzyme that catalyzes the flavin mononucleotide-dependent formation of orotic acid, a key step in de novo pyrimidine biosynthesis |
711913 |
1.3.5.2 | physiological function |
the enzyme is involved in de novo biosynthesis of pyrimidines |
712147 |
1.3.5.2 | physiological function |
the enzyme is involved in de novo biosynthesis of pyrimidines, which is essential in malaria. Absence of pyrimidine salvage pathways in Plasmodium, thus the de novo pathway provides the only source of pyrimidines for cell growth. The mitochondrial enzyme requires oxidized ubiquinone, thus coupling pyrimidine biosynthesis to the respiratory chain |
712147 |
1.3.5.2 | physiological function |
the gene appears to be essential, because while gene tagging is successful at the TgDHOD gene locus, attempts to delete the TgDHOD gene were not successful in the KU80 background |
725919 |