Structural characteristics and catalytic cycle of dihydroorotate dehydrogenase-a review.

Author: Xiaoli REN ¹ ; Fen LUO ² ; Xixi LI ¹ ; Sha YI ¹ ; Bing YANG ¹ ; Zhiyong JIANG ¹
Author Information

1. Food and Drug Teaching and Research Department, School of Environment and Quality Testing, Chongqing Chemical Industry Vocational College, Chongqing 401228, China.
2. Research Institute of Surgery and Daping Hospital, Third Military Medical University, Chongqing 400042, China.
Publication Type:Review
Keywords: catalytic cycle; dihydroorotate dehydrogenase; novel coronavirus; rheumatoid arthritis; structure characteristics
MeSH: Catalysis; Mitochondria/metabolism*; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors/metabolism*
From: Chinese Journal of Biotechnology 2020;36(12):2732-2740
CountryChina
Language:Chinese
Abstract: Dihydroorotate dehydrogenase is a flavin-dependent mitochondrial enzyme to catalyze the fourth step of the de novo synthesis of pyrimidine and to oxidize dihydroorotate to orotate. By selectively inhibiting dihydroorotate dehydrogenase, thereby inhibiting pyrimidine synthesis, the enzyme has been developed for the treatment of cancer, autoimmune diseases, bacterial or viral infections, parasitic diseases and so on. The development of inhibitory drugs requires a detailed understanding of the structural characteristics and catalytic cycle mechanism of dihydroorotate dehydrogenase. Therefore, this paper reviews these two aspects, and indicates perspectives of these inhibitors in clinical application.