期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 632, 期 -, 页码 175-191出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2017.06.019
关键词
Dihydroorotate dehydrogenase; Flavoenzyme; Pyrimidine biosynthesis; Drug target
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [FAPESP] [2012/25075-0, 2011/23504-9, 2004/14407-6, 2004/12349-9, 2005/58008-0, 2007/08703-00]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico [CNPq] [308058/2012-7, 140445/2016-1]
The flavoenzyme dihydroorotate dehydrogenase catalyzes the stereoselective oxidation of (S)-dihydroorotate to orotate in the fourth of the six conserved enzymatic reactions involved in the de novo pyrimidine biosynthetic pathway. Inhibition of pyrimidine metabolism by selectively targeting DHODHs has been exploited in the development of new therapies against cancer, immunological disorders, bacterial and viral infections, and parasitic diseases. Through a chronological narrative, this review summarizes the efforts of the scientific community to achieve our current understanding of structural and biochemical properties of DHODHs. It also attempts to describe the latest advances in medicinal chemistry for therapeutic development based on the selective inhibition of DHODH, including an overview of the experimental techniques used for ligand screening during the process of drug discovery. (C) 2017 Elsevier Inc. All rights reserved.
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