| Author/Editor | Ullrich, Alexandra; Knecht, Wolfgang; Piškur, Jure; Loffler, Monika | |
| Title | Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes | |
| Type | članek | |
| Source | FEBS Lett | |
| Vol. and No. | Letnik 529, št. 2-3 | |
| Publication year | 2002 | |
| Volume | str. 346-50 | |
| Language | eng | |
| Abstract | 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. | |
| Descriptors | AMINO ACID SEQUENCE ARABIDOPSIS BASE SEQUENCE DNA PRIMERS DNA, COMPLEMENTARY ELECTROPHORESIS, POLYACRYLAMIDE GEL KINETICS MOLECULAR SEQUENCE DATA OXIDOREDUCTASES RECOMBINANT PROTEINS SEQUENCE HOMOLOGY, AMINO ACID SEQUENCE HOMOLOGY, NUCLEIC ACID SUBSTRATE SPECIFICITY |