title: Crystallization and preliminary X-ray diffraction analysis of thermophilic imidase from pig liver.
abstract: 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 A, alpha = 82.10, beta = 72.54, gamma = 77.19 degrees, and the other belongs to the orthorhombic C222(1) space group, with unit-cell parameters a = 113.92, b = 157.22, c = 156.21 A.
authors.affiliation: Department of Biological Science and Technology, College of Science, National Chiao Tung University, Hsinchu, Taiwan.
authors.forename: Cheng-Yang
authors.initials: CY
authors.lastname: Huang
authors.forename: Sheng-Kuo
authors.initials: SK
authors.lastname: Chiang
authors.forename: Yuh-Shyong
authors.initials: YS
authors.lastname: Yang
authors.forename: Yuh-Ju
authors.initials: YJ
authors.lastname: Sun
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D004795:Enzyme Stability; D006358:Hot Temperature; D008099:Liver / Q000201:enzymology*; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D000581:Amidohydrolases; C020047:dihydropyrimidinase