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Molecules. 2021 Nov 29;26(23). doi: 10.3390/molecules26237249.

Structural Analysis of .

Molecules (Basel, Switzerland)

Hong-Hsiang Guan, Yen-Hua Huang, En-Shyh Lin, Chun-Jung Chen, Cheng-Yang Huang

Affiliations

  1. Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 33076, Taiwan.
  2. School of Biomedical Sciences, Chung Shan Medical University, No.110, Sec.1, Chien-Kuo N. Rd., Taichung City 402, Taiwan.
  3. Department of Beauty Science, National Taichung University of Science and Technology, No.193, Sec.1, San-Min Rd., Taichung City 403, Taiwan.
  4. Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan City 701, Taiwan.
  5. Department of Physics, National Tsing Hua University, Hsinchu 30043, Taiwan.
  6. Department of Biological Science and Technology, National Chiao Tung University, Hsinchu 300193, Taiwan.
  7. Department of Medical Research, Chung Shan Medical University Hospital, No.110, Sec.1, Chien-Kuo N. Rd., Taichung City 402, Taiwan.

PMID: 34885830 DOI: 10.3390/molecules26237249

Abstract

Dihydroorotase (DHOase), a dimetalloenzyme containing a carbamylated lysine within the active site, is a member of the cyclic amidohydrolase family, which also includes allantoinase (ALLase), dihydropyrimidinase (DHPase), hydantoinase, and imidase. Unlike most known cyclic amidohydrolases, which are tetrameric, DHOase exists as a monomer or dimer. Here, we report and analyze two crystal structures of the eukaryotic

Keywords: CAD; allantoinase; dihydroorotase; dihydropyrimidinase; pyrimidine biosynthesis; tetramerization; thermostability

Publication Types

Grant support