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

FEBS Letters

Piskur, Jure²  Knecht, Wolfgang²  Löffler, Monika¹  Ullrich, Alexandra¹ 

[1]Institute for Physiological Chemistry, Philipps-University, Karl-von-Frisch-Str. 1, D-35033 Marburg, Germany

[2]BioCentrum, Technical University of Denmark, DK-2800 Lyngby, Denmark

关键词: Dihydroorotate dehydrogenase;    Pyrimidines;    Quinones;    Recombinant;    Arabidopsis thaliana;    DHODH;    dihydroorotate dehydrogenase (EC 1.3.99.11);    DHO;    L-dihydroorotate;    QD;    decylubiquinone;    Q10;    ubiquinone-50;    PQD;    decylplastoquinone;    PQ0;    2;    5-dimethyl-p-benzoquinone;    DCIP;    2;    6-dichlorophenol-indophenol;   

DOI  :  10.1016/S0014-5793(02)03425-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown