標題: Crystallization and preliminary X-ray diffraction analysis of thermophilic imidase from pig liver
作者: Huang, CY
Chiang, SK
Yang, YS
Sun, YJ
生物科技學系
Department of Biological Science and Technology
公開日期: 1-May-2003
摘要: Imidase is an enzyme, also known as dihydropyrimidinase (EC 3.5.2.2), hydantoinase, dihydropyrimidine hydrase or dihydropyrimidine amidohydrolase, that catalyzes the reversible hydrolysis of 5,6-dihydrouracil to 3-ureidopropionate and many other imides. Substrate specificity, metal content and amino-acid sequence all differ significantly between bacterial and mammalian imide-hydrolyzing enzymes. In this study, a thermophilic imidase was isolated from pig liver and crystallized. Two kinds of imidase crystals were grown by the hanging-drop vapour-diffusion method using polyethylene glycol MME 5000 and 2-propanol as precipitants. One belongs to the triclinic P-1 space group, with unit-cell parameters a = 96.35, b = 96.87, c = 154.87 Angstrom, alpha = 82.10, beta = 72.54, gamma = 77.19degrees, and the other belongs to the orthorhombic C222(1) space group, with unit-cell parameters a = 113.92, b = 157.22, c = 156.21 Angstrom.
URI: http://dx.doi.org/10.1107/S090744490300578X
http://hdl.handle.net/11536/27882
ISSN: 0907-4449
DOI: 10.1107/S090744490300578X
期刊: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume: 59
Issue: 
起始頁: 943
結束頁: 945
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