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Crystallization and preliminary X-ray diffraction analysis of thermophilic imidase from pig liver.
- Source :
- Acta Crystallographica: Section D (Wiley-Blackwell); May2003, Vol. 59 Issue 5, p943, 3p
- Publication Year :
- 2003
-
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 contem 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[SUB1] space group, with unit-cell parameters a = 9635, b = 96.87. c = 154.87 Å, a = 82.10, β = 72.54, γ = 77.19°, and the other belongs to the orthorhombic C222[SUB1] space group, with unit-cell parameters a = 113.92, b = 157.22, c = 156.21 Å. [ABSTRACT FROM AUTHOR]
- Subjects :
- ENZYMES
LIVER
SWINE
CRYSTALLIZATION
Subjects
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 59
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 9808069
- Full Text :
- https://doi.org/10.1107/S0907444903005912